D. Winge

发表

Sulfide stabilization of the cadmium-gamma-glutamyl peptide complex of Schizosaccharomyces pombe.

R. Reese, D. Winge, 1988, The Journal of biological chemistry.

Yeast Contain a Non-proteinaceous Pool of Copper in the Mitochondrial Matrix*

D. Winge, P. Cobine, Luis Ojeda, 2004, Journal of Biological Chemistry.

Identification of the Copper Regulon in Saccharomyces cerevisiae by DNA Microarrays*

P. Brown, V. Iyer, D. Winge, 2000, The Journal of Biological Chemistry.

Pet191 Is a Cytochrome c Oxidase Assembly Factor in Saccharomyces cerevisiae

D. Winge, P. Cobine, K. Rigby, 2008, Eukaryotic Cell.

The LYR Protein Mzm1 Functions in the Insertion of the Rieske Fe/S Protein in Yeast Mitochondria

D. Winge, O. Khalimonchuk, Aaron E. Atkinson, 2011, Molecular and Cellular Biology.

Copper trafficking to the mitochondrion and assembly of copper metalloenzymes.

D. Winge, P. Cobine, F. Pierrel, 2006, Biochimica et biophysica acta.

The Zap1 transcriptional activator also acts as a repressor by binding downstream of the TATA box in ZRT2

D. Stillman, D. Winge, D. Eide, 2004, The EMBO journal.

Distinct metal binding configurations in ACE1.

D. Winge, G. George, C. Dameron, 1993, Biochemistry.

Protein-mediated assembly of succinate dehydrogenase and its cofactors

D. Winge, J. Rutter, Jonathan G Van Vranken, 2015, Critical reviews in biochemistry and molecular biology.

Emerging concepts in the flavinylation of succinate dehydrogenase.

D. Winge, H. Kim, 2013, Biochimica et biophysica acta.

Metal acquisition and availability in the mitochondria.

D. Winge, Aaron E. Atkinson, 2009, Chemical reviews.

Sequence and antigenicity of calf metallothionein II.

D. Winge, W. Gray, A. Żelazowski, 1986, Archives of biochemistry and biophysics.

A targetable fluorescent sensor reveals that copper-deficient SCO1 and SCO2 patient cells prioritize mitochondrial copper homeostasis.

Christopher J. Chang, D. Winge, S. C. Leary, 2011, Journal of the American Chemical Society.

Mitochondrial cardiomyopathies feature increased uptake and diminished efflux of mitochondrial calcium.

D. Winge, Mi-Young Jeong, S. Sommakia, 2017, Journal of molecular and cellular cardiology.

The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis.

E. Shoubridge, P. Rustin, D. Winge, 2007, Cell metabolism.

Characterization of the copper chaperone Cox17 of Saccharomyces cerevisiae.

M. Posewitz, D. Winge, G. George, 1998, Biochemistry.

Mutational Analysis of the Mitochondrial Copper Metallochaperone Cox17*

D. Winge, C. Srinivasan, T. Nittis, 2000, The Journal of Biological Chemistry.

Yeast Sco1, a Protein Essential for Cytochrome cOxidase Function Is a Cu(I)-binding Protein*

D. Winge, G. George, T. Nittis, 2001, The Journal of Biological Chemistry.

Yeast Cox11, a Protein Essential for Cytochrome cOxidase Assembly, Is a Cu(I)-binding Protein*

D. Winge, G. George, H. Carr, 2002, The Journal of Biological Chemistry.

Erratum: Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae (Journal of Biological Chemistry (1998) 273 (23716-23721))

D. Winge, L. T. Jensen, J. R. Simon, 1998 .

Modeling Human Protein Aggregation Cardiomyopathy Using Murine Induced Pluripotent Stem Cells

D. Srivastava, Kathryn N. Ivey, I. Benjamin, 2013, Stem cells translational medicine.

Host defenses against copper toxicity.

R. Mehra, D. Winge, D. R. Winge, 1990, International review of experimental pathology.

Cox17 Is Functional When Tethered to the Mitochondrial Inner Membrane*

D. Winge, Dennis R Winge, Andrew B Maxfield, 2004, Journal of Biological Chemistry.

Mapping the Functional Interaction of Sco1 and Cox2 in Cytochrome Oxidase Biogenesis*

D. Winge, P. Cobine, K. Rigby, 2008, Journal of Biological Chemistry.

Characterization of the Cytochrome c Oxidase Assembly Factor Cox19 of Saccharomyces cerevisiae*

D. Winge, P. Cobine, K. Rigby, 2007, Journal of Biological Chemistry.

Human Sco1 and Sco2 Function as Copper-binding Proteins*

E. Shoubridge, D. Winge, S. C. Leary, 2005, Journal of Biological Chemistry.

Specific Copper Transfer from the Cox17 Metallochaperone to Both Sco1 and Cox11 in the Assembly of Yeast Cytochrome c Oxidase*

D. Winge, P. Cobine, H. Carr, 2004, Journal of Biological Chemistry.

Reprint of: Biogenesis of the cytochrome bc(1) complex and role of assembly factors.

D. Winge, Pamela M. Smith, J. L. Fox, 2012, Biochimica et biophysica acta.

Biogenesis of the cytochrome bc(1) complex and role of assembly factors.

D. Winge, Pamela M. Smith, J. L. Fox, 2012, Biochimica et biophysica acta.

Iron-Mediated Inhibition of Mitochondrial Manganese Uptake Mediates Mitochondrial Dysfunction in a Mouse Model of Hemochromatosis

D. Winge, R. Cooksey, D. McClain, 2008, Molecular medicine.

Structure of human Fe–S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP–ISD11 interactions

D. Winge, E. Brignole, J. Rutter, 2017, Proceedings of the National Academy of Sciences.

Mutated Yeast Heat Shock Transcription Factor Exhibits Elevated Basal Transcriptional Activation and Confers Metal Resistance (*)

D. Winge, A. Sewell, Wei Yu, 1995, The Journal of Biological Chemistry.

Manganese supplementation protects against diet-induced diabetes in wild type mice by enhancing insulin secretion.

D. Winge, R. Cooksey, Deborah L Jones, 2013, Endocrinology.

Isolated Cytochrome c Oxidase Deficiency in G93A SOD1 Mice Overexpressing CCS Protein*

D. Winge, R. Haller, F. Pierrel, 2008, Journal of Biological Chemistry.

Crystals of cadmium, zinc metallothionein.

D. Winge, C. Stout, D. Carter, 1984, Environmental health perspectives.

Isolation of copper thionein from rat liver.

D. Winge, B. Geller, J. Garvey, 1981, Archives of biochemistry and biophysics.

Copper coordination in metallothionein.

D. Winge, 1991, Methods in enzymology.

Copper-chelatin: purification and properties of a copper-binding protein from rat liver.

R. D. Wiley, D. Winge, K. Rajagopalan, 1975, Archives of biochemistry and biophysics.

Mixed Cu+ and Zn2+ coordination in the DNA-binding domain of the AMT1 transcription factor from Candida glabrata.

J. Peltier, D. Winge, A. Sewell, 1994, Biochemistry.

Cuprous-Thiolate Polymetalic Clusters in Biology

D. Winge, G. George, I. Pickering, 1993 .

Selective and tandem amplification of a member of the metallothionein gene family in Candida glabrata.

R. Mehra, D. Winge, J. Garey, 1990, The Journal of biological chemistry.

A copper-thiolate polynuclear cluster in the ACE1 transcription factor.

D. Hamer, D. Winge, G. George, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Metal Ion availability in mitochondria

D. Winge, P. Cobine, F. Pierrel, 2007, BioMetals.

Purification and some properties of Cd-binding protein from rat liver.

D. Winge, K. Rajagopalan, 1972, Archives of biochemistry and biophysics.

Protection against cadmium toxicity in yeast by alcohol dehydrogenase.

D. Winge, I. Macreadie, W. Yu, 1991, Journal of inorganic biochemistry.

Juxtaposition of chemical and mutation-induced developmental defects in zebrafish reveal a copper-chelating activity for kalihinol F.

D. Winge, E. Manos, David A Jones, 2013, Chemistry & biology.

Copper-chelatin: isolation from various eucaryotic sources.

R. D. Wiley, D. Winge, K. Rajagopalan, 1975, Archives of biochemistry and biophysics.

Structural and functional diversity of copper-metallothioneins from the American lobster Homarus americanus.

D. Winge, M. Brouwer, W. Gray, 1989, Journal of inorganic biochemistry.

Role of the conserved histidines in the Zn module of the copper-activated transcription factors in yeast

M. Posewitz, D. Winge, J. R. Simon, 1996, JBIC Journal of Biological Inorganic Chemistry.

Disruption analysis of metallothionein-encoding genes in Candida glabrata.

R. Mehra, D. Winge, I. Macreadie, 1992, Gene.

Cloning system for Candida glabrata using elements from the metallothionein-IIa-encoding gene that confer autonomous replication.

R. Mehra, D. Winge, I. Macreadie, 1992, Gene.

Oxygen-dependent activation of Cu,Zn-superoxide dismutase-1.

D. Winge, Duane D. Winkler, Stefanie Boyd, 2017, Metallomics : integrated biometal science.

The Plasma Membrane Protein Nce102 Implicated in Eisosome Formation Rescues a Heme Defect in Mitochondria*

D. Winge, Mi-Young Jeong, J. Phillips, 2016, The Journal of Biological Chemistry.

Copper Modulates the Differentiation of Mouse Hematopoietic Progenitor Cells in Culture

D. Winge, P. Cobine, G. Spangrude, 2009, Cell transplantation.

Metal-induced formation of metallothionein in rat liver.

D. Winge, K. Rajagopalan, R. Premakumar, 1975, Archives of biochemistry and biophysics.

Studies on the zinc content of Cd-induced thionein.

D. Winge, K. Rajagopalan, R. Premakumar, 1978, Archives of Biochemistry and Biophysics.

Common metal ion coordination in LIM domain proteins.

H. A. Louis, M. Beckerle, D. Winge, 1994, Biochemistry.

Coa2 Is an Assembly Factor for Yeast Cytochrome c Oxidase Biogenesis That Facilitates the Maturation of Cox1

D. Winge, P. Cobine, O. Khalimonchuk, 2008, Molecular and Cellular Biology.

Coa 2 Is an Assembly Factor for Yeast Cytochrome c Oxidase Biogenesis That Facilitates the Maturation of Cox 1

D. Winge, P. Cobine, O. Khalimonchuk, 2008 .

Function and redox state of mitochondrial localized cysteine-rich proteins important in the assembly of cytochrome c oxidase.

D. Winge, O. Khalimonchuk, 2008, Biochimica et biophysica acta.

Structural studies of the heme domain of sulfite oxidase: CNBr fragments.

W. Southerland, D. Winge, K. Rajagopalan, 1978, Biochemistry.

Copper- and silver-substituted yeast metallothioneins: sequential 1H NMR assignments reflecting conformational heterogeneity at the C terminus.

D. Winge, I. Armitage, S. Narula, 1993, Biochemistry.

Flavinylation and Assembly of Succinate Dehydrogenase Are Dependent on the C-terminal Tail of the Flavoprotein Subunit*

D. Winge, Mi-Young Jeong, Un Na, 2012, The Journal of Biological Chemistry.

Formation of the Redox Cofactor Centers during Cox1 Maturation in Yeast Cytochrome Oxidase

D. Winge, O. Khalimonchuk, B. Meunier, 2009, Molecular and Cellular Biology.

The Role of Coa2 in Hemylation of Yeast Cox1 Revealed by Its Genetic Interaction with Cox10

D. Winge, O. Khalimonchuk, Megan L. Bestwick, 2009, Molecular and Cellular Biology.

Sealing the Mitochondrial Respirasome

D. Winge, 2012, Molecular and Cellular Biology.

Cox1 mutation abrogates need for Cox23 in cytochrome c oxidase biogenesis

D. Winge, Mi-Young Jeong, R. D. Dela Cruz, 2016, Microbial cell.

2016A Dela Cruz Microbial Cell

D. Winge, Mi-Young Jeong, R. D. Dela Cruz, 2016 .

Selective Oma1 Protease-mediated Proteolysis of Cox1 Subunit of Cytochrome Oxidase in Assembly Mutants*

D. Winge, Mi-Young Jeong, E. Ferris, 2012, The Journal of Biological Chemistry.

Subcellular distribution of superoxide dismutases in rat liver.

D. Winge, B. Geller, 1984, Methods in enzymology.

Uptake of cadmium-109, a metallothionein-binding radiometal, by tumors in mice as a function of the transformed phenotype.

D. Winge, F. Datz, A. Taylor, 1988, Investigative radiology.

X-ray absorption studies of yeast copper metallothionein.

D. Winge, J. Byrd, G. George, 1988, The Journal of biological chemistry.

Characterization of the copper-thiolate cluster in yeast metallothionein and two truncated mutants.

D. Hamer, D. Winge, D. McMillin, 1988, The Journal of biological chemistry.

N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization

D. Winge, M. Cygler, R. Lill, 2021, Nature Communications.

Bioactivity of metallothionein-3 correlates with its novel beta domain sequence rather than metal binding properties.

R. Palmiter, D. Winge, A. Sewell, 1995, Biochemistry.

Limited proteolysis of metallothioneins.

D. Winge, 1991, Methods in enzymology.

Effect of the two conserved prolines of human growth inhibitory factor (metallothionein-3) on its biological activity and structure fluctuation: comparison with a mutant protein.

D. Winge, L. T. Jensen, O. Zerbe, 2000, Biochemistry.

Analysis of copper‐induced metallothionein expression using autonomously replicating plasmids in Candida glabrata

R. Mehra, D. Winge, A. Sewell, 1995, Yeast.

Discussion Summary. Techniques and Problems in Metal-Binding Protein Chemistry and Implications for Proteins in Nonmammalian Organisms

D. Winge, M. Brouwer, 1986 .

Techniques and problems in metal-binding protein chemistry and implications for proteins in nonmammalian organisms.

D. Winge, M. Brouwer, 1986, Environmental health perspectives.

Metal binding sites of rat liver Cu-thionein.

D. Winge, B. Geller, D. R. Winge, 1982, Archives of biochemistry and biophysics.

Late-Stage Maturation of the Rieske Fe/S Protein: Mzm1 Stabilizes Rip1 but Does Not Facilitate Its Translocation by the AAA ATPase Bcs1

D. Winge, O. Khalimonchuk, Pamela M. Smith, 2012, Molecular and Cellular Biology.

Analysis of Leigh Syndrome Mutations in the Yeast SURF1 Homolog Reveals a New Member of the Cytochrome Oxidase Assembly Factor Family

D. Winge, Mi-Young Jeong, O. Khalimonchuk, 2010, Molecular and Cellular Biology.

Phosphate starvation signaling increases mitochondrial membrane potential through respiration-independent mechanisms

S. Gygi, D. Winge, J. Rutter, 2022, bioRxiv.

The domains of rat liver sulfite oxidase. Proteolytic separation and characterization.

W. Southerland, D. Winge, K. Rajagopalan, 1978, The Journal of biological chemistry.

Glutathione-coated cadmium-sulfide crystallites in Candida glabrata.

D. Winge, C. Dameron, B. R. Smith, 1989, The Journal of biological chemistry.

The Janus face of copper: its expanding roles in biology and the pathophysiology of disease

D. Winge, S. Leary, 2007, EMBO reports.

Modulation of the Respiratory Supercomplexes in Yeast

D. Winge, J. L. Fox, Tie-Zhong Cui, 2014, The Journal of Biological Chemistry.

Transcription of the Yeast Iron Regulon Does Not Respond Directly to Iron but Rather to Iron-Sulfur Cluster Biosynthesis*

M. Bard, D. Winge, M. Valachovič, 2004, Journal of Biological Chemistry.

Metal Ions in Fungi

D. Winge, D. Griffin, G. Winkelmann, 1995 .

Order of metal binding in metallothionein.

D. Winge, K. Nielson, D. R. Winge, 1983, The Journal of biological chemistry.

The effects of mitochondrial iron homeostasis on cofactor specificity of superoxide dismutase 2

D. Winge, Mei Yang, V. Culotta, 2006, The EMBO journal.

Formation of the metal-thiolate clusters of rat liver metallothionein.

D. Winge, K. Nielson, D. R. Winge, 1984, Environmental health perspectives.

Metal ion resistance in fungi: Molecular mechanisms and their regulated expression

R. Mehra, D. Winge, 1991, Journal of cellular biochemistry.

Metalloregulation of FRE1 and FRE2Homologs in Saccharomyces cerevisiae *

D. Winge, L. T. Jensen, J. R. Simon, 1998, The Journal of Biological Chemistry.

A method for distinguishing Cu,Zn- and Mn-containing superoxide dismutases.

D. Winge, B. Geller, 1983, Analytical biochemistry.

Crystal structure of Cd,Zn metallothionein.

B. Wang, D. Winge, C. Stout, 1985, Science.

Copper-induced synthesis of copper-chelatin in rat liver.

R. D. Wiley, D. Winge, K. Rajagopalan, 1975, Archives of biochemistry and biophysics.

X-ray absorption studies of the copper-beta domain of rat liver metallothionein.

D. Winge, C. Stout, G. George, 1986, Journal of inorganic biochemistry.

113Cd NMR study of a metallothionein fragment. Evidence for a two-domain structure.

D. Winge, Y. Boulanger, I. Armitage, 1982, The Journal of biological chemistry.

Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site

D. Winge, P. Hart, J. Wohlschlegel, 2017, The Journal of Biological Chemistry.

Yeast metallothionein. Sequence and metal-binding properties.

D. Hamer, D. Winge, W. Gray, 1985, The Journal of biological chemistry.

Structure, function, and assembly of heme centers in mitochondrial respiratory complexes.

D. Winge, O. Khalimonchuk, Pamela M. Smith, 2012, Biochimica et biophysica acta.

Domain nature of metallothionein.

D. Winge, K. Miklóssy, 1982, The Journal of biological chemistry.

Preferential binding of copper to the beta domain of metallothionein.

D. Winge, K. Nielson, Dennis R. WingeS, 1984, The Journal of biological chemistry.

Antigenicity of metallothionein.

D. Winge, J. Garvey, 1983, Proceedings of the National Academy of Sciences of the United States of America.

The Characterization and Role of Zinc Binding in Yeast Cox4*

I. Bertini, D. Winge, L. Banci, 2007, Journal of Biological Chemistry.

Evidence for a Pro-oxidant Intermediate in the Assembly of Cytochrome Oxidase*

D. Winge, O. Khalimonchuk, A. Bird, 2007, Journal of Biological Chemistry.

The P174L Mutation in Human Sco1 Severely Compromises Cox17-dependent Metallation but Does Not Impair Copper Binding*

E. Shoubridge, D. Winge, F. Sasarman, 2006, Journal of Biological Chemistry.

X-ray absorption spectroscopy of cuprous-thiolate clusters in proteins and model systems

D. Winge, G. George, I. Pickering, 1993 .

Copper metallochaperones.

D. Winge, N. Robinson, 2010, Annual review of biochemistry.

Distinct metal-binding configurations in metallothionein.

D. Winge, C. Atkin, K. Nielson, 1985, The Journal of biological chemistry.

Cadmium accumulation in rat liver.

D. Winge, A. Colucci, J. Krasno, 1975, Archives of environmental health.

Biosynthesis of cadmium sulphide quantum semiconductor crystallites

M. Steigerwald, A. Kortan, R. Mehra, 1989, Nature.

Long-term turnover of cadmium metallothionein in liver and kidney following a single low dose of cadmium in rats.

B. Fowler, D. Winge, J. Ridlington, 1981, Biochimica et biophysica acta.

Preferential binding of copper to the β domain of metallothionein

D. Winge, K. Nielson, 1984 .

Cu(I) binding to the Schizosaccharomyces pombe γ-glutamyl peptides varying in chain lengths

R. Mehra, D. Winge, 1988 .

Mammalian metal response element-binding transcription factor-1 functions as a zinc sensor in yeast, but not as a sensor of cadmium or oxidative stress.

D. Winge, G. Andrews, D. Bittel, 2002, Nucleic acids research.

Characterization of a human chorionic gonadotropin-like protein from Candida albicans.

D. Winge, W. Odell, Y. Li, 1993, Endocrinology.

Structures of the cuprous-thiolate clusters of the Mac1 and Ace1 transcriptional activators.

D. Winge, H. Harris, G. George, 2002, Biochemistry.

Cadmium-Sulfide Crystallites in Cd-(γEC)nG Peptide Complexes from Tomato

R. Reese, D. Winge, C. A. White, 1992 .

A Novel Role for Copper in Ras/Mitogen-Activated Protein Kinase Signaling

D. Thiele, D. Winge, C. Counter, 2012, Molecular and Cellular Biology.

Functional Analysis of the Domains in Cox11*

D. Winge, H. Carr, Y. Horng, 2005, Journal of Biological Chemistry.

Copper-regulatory domain involved in gene expression.

D. Winge, 1998, Progress in nucleic acid research and molecular biology.

Zap1 activation domain 1 and its role in controlling gene expression in response to cellular zinc status

D. Winge, D. Eide, A. Bird, 2005, Molecular microbiology.

Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRP

H. A. Louis, M. Beckerle, M. Summers, 1994, Nature Structural Biology.

Mne1 Is a Novel Component of the Mitochondrial Splicing Apparatus Responsible for Processing of a COX1 Group I Intron in Yeast*

Rachel Z. Wolf, G. Mohr, D. Winge, 2011, The Journal of Biological Chemistry.

Identification of SLF1 as a new copper homeostasis gene involved in copper sulfide mineralization in Saccharomyces cerevisiae

D. Stillman, D. Winge, W. Yu, 1996, Molecular and cellular biology.

Metal Ion Stress in Yeast

D. Winge, A. Sewell, Wei Yu, 1998 .

COX19 mediates the transduction of a mitochondrial redox signal from SCO1 that regulates ATP7A-mediated cellular copper efflux

E. Shoubridge, M. Tarnopolsky, D. Winge, 2013, Molecular biology of the cell.

Copper-regulatory domain involved in gene expression.

D. Winge, 1999, Advances in experimental medicine and biology.

Mapping the DNA Binding Domain of the Zap1 Zinc-responsive Transcriptional Activator*

D. Winge, D. Eide, Hui Zhao, 2000, The Journal of Biological Chemistry.

Regulation of the Yeast TSA1 Peroxiredoxin by ZAP1 Is an Adaptive Response to the Oxidative Stress of Zinc Deficiency*

D. Winge, D. Eide, Dennis R Winge, 2007, Journal of Biological Chemistry.

An extracellular histidine-containing motif in the zinc transporter ZIP4 plays a role in zinc sensing and zinc-induced endocytosis in mammalian cells

D. Winge, Byung-Eun Kim, Chul-Jin Lee, 2018, The Journal of Biological Chemistry.

Rat liver Cu,Zn-superoxide dismutase. Subcellular location in lysosomes.

D. Winge, B. Geller, 1982, The Journal of biological chemistry.

Copper-mediated repression of the activation domain in the yeast Mac1p transcription factor.

D. Winge, J. A. Graden, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Candida glabrata metallothioneins. Cloning and sequence of the genes and characterization of proteins.

R. Mehra, D. Winge, T. Butt, 1989, The Journal of biological chemistry.

SDH5, a Gene Required for Flavination of Succinate Dehydrogenase, Is Mutated in Paraganglioma

Steven P. Gygi, Peter Devilee, Jared Rutter, 2009, Science.

ACP Acylation Is an Acetyl-CoA-Dependent Modification Required for Electron Transport Chain Assembly.

Katie J. Clowers, S. Gygi, D. Winge, 2018, Molecular cell.

Haa1, a Protein Homologous to the Copper-regulated Transcription Factor Ace1, Is a Novel Transcriptional Activator*

P. Brown, D. Winge, G. Keller, 2001, The Journal of Biological Chemistry.

Mitochondrial fatty acid synthesis coordinates oxidative metabolism in mammalian mitochondria

Sara M. Nowinski, Bradley C. Naylor, S. Gygi, 2020, eLife.

The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis

S. Gygi, D. Winge, J. Rutter, 2016, eLife.

“ Pulling the plug ” on cellular copper : The role of mitochondria in copper export

D. Winge, P. Cobine, S. Leary, 2008 .

Coa1 links the Mss51 post‐translational function to Cox1 cofactor insertion in cytochrome c oxidase assembly

D. Winge, P. Cobine, O. Khalimonchuk, 2007, The EMBO journal.

Mitochondrial Matrix Copper Complex Used in Metallation of Cytochrome Oxidase and Superoxide Dismutase*

D. Winge, P. Cobine, Megan L. Bestwick, 2006, Journal of Biological Chemistry.

Cbp3 and Cbp6 are dispensable for synthesis regulation of cytochrome b in yeast mitochondria

D. Winge, X. Pérez-Martínez, Angélica Zamudio-Ochoa, 2018, The Journal of Biological Chemistry.

Sequestration of cadmium and copper by recombinant rainbow trout and human metallothioneins and by chimeric (mermaid and fishman) proteins with interchanged domains.

D. Winge, P. Kille, W. E. Lees, 1992, The Journal of biological chemistry.

Differential control of Zap1-regulated genes in response to zinc deficiency in Saccharomyces cerevisiae

M. Newton, D. Winge, D. Eide, 2008, BMC Genomics.

Repression of ADH1 and ADH3 during zinc deficiency by Zap1‐induced intergenic RNA transcripts

D. Winge, D. Eide, A. Bird, 2006, The EMBO journal.

Analysis of SDHAF3 in familial and sporadic pheochromocytoma and paraganglioma

Katherine M. Tucker, T. Dwight, D. Winge, 2017, BMC Cancer.

Succinate dehydrogenase - Assembly, regulation and role in human disease.

D. Winge, J. Schiffman, J. Rutter, 2010, Mitochondrion.

Loss of Cardiolipin Leads to Perturbation of Mitochondrial and Cellular Iron Homeostasis*

D. Winge, Vinay A Patil, Vishal M. Gohil, 2012, The Journal of Biological Chemistry.

Zinc fingers can act as Zn2+ sensors to regulate transcriptional activation domain function

D. Winge, D. Eide, A. Bird, 2003, The EMBO journal.

Thiol peroxidases mediate specific genome-wide regulation of gene expression in response to hydrogen peroxide

V. Gladyshev, D. Fomenko, D. Winge, 2011, Proceedings of the National Academy of Sciences.

Zinc binding to a regulatory zinc-sensing domain monitored in vivo by using FRET.

D. Winge, D. Eide, Dennis R Winge, 2006, Proceedings of the National Academy of Sciences of the United States of America.

The LIM motif defines a specific zinc-binding protein domain.

M. Beckerle, K. Schmeichel, D. Winge, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Differences in the polymorphic forms of metallothionein.

D. Winge, K. Miklóssy, 1982, Archives of biochemistry and biophysics.

The Zap 1 transcriptional activator also acts as a repressor by binding downstream of the TATA box in ZRT 2

D. Stillman, D. Winge, D. Eide, 2013 .

Repression of Sulfate Assimilation Is an Adaptive Response of Yeast to the Oxidative Stress of Zinc Deficiency*

D. Winge, D. Eide, S. Roje, 2009, The Journal of Biological Chemistry.

Enhanced neurotrophic activity in Alzheimer's disease cortex is not associated with down-regulation of metallothionein-III (GIF)

R. Palmiter, D. Winge, A. Sewell, 1994, Brain Research.

Structure of the cysteine-rich intestinal protein, CRIP.

H. A. Louis, M. Beckerle, M. Summers, 1996, Journal of molecular biology.

Independent Metalloregulation of Ace1 and Mac1 in Saccharomyces cerevisiae

D. Winge, A. Bird, Amanda J. Bird, 2005, Eukaryotic Cell.

Zinc-Regulated DNA Binding of the Yeast Zap1 Zinc-Responsive Activator

D. Winge, D. Eide, A. Bird, 2011, PloS one.

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.

Role of Glutaredoxin-3 and Glutaredoxin-4 in the Iron Regulation of the Aft1 Transcriptional Activator in Saccharomyces cerevisiae*

D. Winge, Luis Ojeda, R. Lill, 2006, Journal of Biological Chemistry.

Activation of the Iron Regulon by the Yeast Aft1/Aft2 Transcription Factors Depends on Mitochondrial but Not Cytosolic Iron-Sulfur Protein Biogenesis*

D. Winge, Luis Ojeda, J. Balk, 2005, Journal of Biological Chemistry.

Aft1p and Aft2p Mediate Iron-responsive Gene Expression in Yeast through Related Promoter Elements*

D. Winge, Dennis R Winge, Julian C Rutherford, 2003, Journal of Biological Chemistry.

Assembly of cytochrome c oxidase within the mitochondrion.

D. Winge, Heather S Carr, Dennis R Winge, 2003, Accounts of chemical research.

Two of the five zinc fingers in the Zap1 transcription factor DNA binding domain dominate site-specific DNA binding.

D G Myszka, D. Winge, D. Eide, 2003, Biochemistry.

A second iron-regulatory system in yeast independent of Aft1p

P. Brown, D. Winge, P O Brown, 2001, Proceedings of the National Academy of Sciences of the United States of America.

A dual role for zinc fingers in both DNA binding and zinc sensing by the Zap1 transcriptional activator

D. Winge, D. Eide, L. T. Jensen, 2000, The EMBO journal.

Identification of a copper‐induced intramolecular interaction in the transcription factor Mac1 from Saccharomyces cerevisiae

D. Winge, L. T. Jensen, D R Winge, 1998, The EMBO journal.

Mapping of the DNA Binding Domain of the Copper-responsive Transcription Factor Mac1 from Saccharomyces cerevisiae *

M. Posewitz, D. Winge, L. T. Jensen, 1998, The Journal of Biological Chemistry.

Presence of a copper(I)-thiolate regulatory domain in the copper-activated transcription factor Amt1.

M. Posewitz, D. Winge, G. George, 1996, Biochemistry.

Identification of the Zn(II) site in the copper-responsive yeast transcription factor, AMT1: a conserved Zn module.

D. Winge, J. Thorvaldsen, R. A. Farrell, 1996, Biochemistry.

Pet 191 is a cytochrome c oxidase assembly factor in Saccharomyces cerevisiae 1

D. Winge, P. Cobine, K. Rigby, 2017 .

LYRM7/MZM1L is a UQCRFS1 chaperone involved in the last steps of mitochondrial Complex III assembly in human cells.

M. Zeviani, D. Winge, E. Fernández-Vizarra, 2013, Biochimica et biophysica acta.

Functional Independence of the Two Cysteine-rich Activation Domains in the Yeast Mac1 Transcription Factor*

D. Winge, C. Gross, G. Keller, 2000, The Journal of Biological Chemistry.

Enhanced Effectiveness of Copper Ion Buffering by CUP1 Metallothionein Compared with CRS5 Metallothionein in Saccharomyces cerevisiae*

D. Winge, W. Howard, L. T. Jensen, 1996, The Journal of Biological Chemistry.

Copper metalloregulation of gene expression.

D. Winge, 2002, Advances in protein chemistry.

Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors

M. Posewitz, M. Summers, D. Winge, 1998, Nature Structural Biology.

Metal-ion regulation of gene expression in yeast.

D. Winge, L. T. Jensen, C. Srinivasan, 1998, Current opinion in chemical biology.

The Yeast Transcription Factor Mac1 Binds to DNA in a Modular Fashion*

D. Winge, L. T. Jensen, T. Tullius, 1999, The Journal of Biological Chemistry.

Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding.

I. Bertini, D. Winge, L. Banci, 2005, Structure.

Steps Toward Understanding Mitochondrial Fe/S Cluster Biogenesis.

D. Winge, A. Melber, 2018, Methods in enzymology.

A persistent untranslated sequence within bacteriophage T4 DNA topoisomerase gene 60.

S. Ao, R. Orlandi, S. Casjens, 1988, Science.

Filling the mitochondrial copper pool

D. Winge, 2018, The Journal of Biological Chemistry.

Copper Import into the Mitochondrial Matrix in Saccharomyces cerevisiae Is Mediated by Pic2, a Mitochondrial Carrier Family Protein*

D. Winge, P. Cobine, S. Leary, 2013, The Journal of Biological Chemistry.

Mitochondrial fatty acid synthesis coordinates mitochondrial oxidative metabolism

Sara M. Nowinski, Bradley C. Naylor, S. Gygi, 2020, bioRxiv.

The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur subunit of succinate dehydrogenase.

C. Thummel, D. Winge, J. Rutter, 2014, Cell metabolism.

Rat Liver Cu,Zn-Superoxide Dismutase

D. Winge, Bruce L. Gellerl, 1982 .

Solution NMR structure of yeast succinate dehydrogenase flavinylation factor Sdh5 reveals a putative Sdh1 binding site.

G. Montelione, J. Prestegard, T. Szyperski, 2012, Biochemistry.

Inner Secrets of the Respirasome

D. Winge, A. Melber, 2016, Cell.

The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex.

D. Winge, G. George, D R Winge, 2001, Biochemistry.

Mzm1 Influences a Labile Pool of Mitochondrial Zinc Important for Respiratory Function*

Oleh Khalimonchuk, D. Winge, D. Eide, 2010, The Journal of Biological Chemistry.

Structure of the human Fe–S cluster assembly sub-complex: implications in Friedreich's ataxia and primary metabolism

D. Winge, E. Brignole, J. Rutter, 2018, Acta Crystallographica Section A Foundations and Advances.

Shaping the mitochondrion: mitochondrial biogenesis, dynamics and dysfunction

J. Shaw, D. Winge, 2009, EMBO reports.

Sensors that mediate copper-specific activation and repression of gene expression

M. Posewitz, D. Winge, L. T. Jensen, 1997, JBIC Journal of Biological Inorganic Chemistry.

Distinct Regions of Cu(I)·ACE1 Contact Two Spatially Resolved DNA Major Groove Sites(*)

D. Hamer, D. Winge, Stella Hu, 1995, The Journal of Biological Chemistry.

Mutational analysis of the metal sites in an LIM domain.

H. A. Louis, M. Beckerle, D. Winge, 1994, The Journal of biological chemistry.

Regulation of metallothionein genes by the ACE1 and AMT1 transcription factors.

D. Winge, A. Sewell, D R Winge, 1993, The Journal of biological chemistry.

Structural characterization of the isoforms of neonatal and adult rat liver metallothionein.

D. Winge, W. Gray, R. Zeikus, 1984, The Journal of biological chemistry.

Engineering of Metallothionein-3 Neuroinhibitory Activity into the Inactive Isoform Metallothionein-1*

D. Winge, L. T. Jensen, O. Zerbe, 2002, The Journal of Biological Chemistry.

Evidence for a dynamic structure of human neuronal growth inhibitory factor and for major rearrangements of its metal-thiolate clusters.

D. Winge, O. Zerbe, P. Faller, 1999, Biochemistry.

Independence of the domains of metallothionein in metal binding.

D. Winge, K. Nielson, 1985, The Journal of biological chemistry.

A plant metallothionein produced in E. coli

D. Winge, P. Kille, J. Harwood, 1991, FEBS letters.

Characterization of peptide-coated cadmium-sulfide crystallites

D. Winge, C. Dameron, 1990 .

Identification of a four copper folding intermediate in mammalian copper metallothionein by electrospray ionization mass spectrometry

J. Peltier, D. Winge, L. T. Jensen, 1998, JBIC Journal of Biological Inorganic Chemistry.

Cooperative cluster formation in metallothionein.

D. Winge, J. Byrd, 1986, Archives of Biochemistry and Biophysics.

Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients

D. Winge, A. Vashisht, J. Wohlschlegel, 2016, eLife.

X‐Ray Absorption Spectroscopy of Cuprous‐Thiolate Clusters in Saccharomyces cerevisiae Metallothionein

D. Winge, G. George, I. Pickering, 2008, Chemistry & biodiversity.

Peptide-mediated formation of quantum semiconductors.

D. Winge, C. Dameron, 1990, Trends in biotechnology.

Mutagenic analysis of Cox11 of Rhodobacter sphaeroides: insights into the assembly of Cu(B) of cytochrome c oxidase.

D. Winge, Aimin Liu, Daniel Smith, 2010, Biochemistry.

Establishment of the Metal-to-Cysteine Connectivities in Silver-Substituted Yeast Metallothionein

R. Mehra, D. Winge, I. Armitage, 1991 .

Mitochondrial Copper Ion Transport

D. Winge, T. Nittis, K. McCall, 2003 .

Zinc Metalloregulation of the Zinc Finger Pair Domain*

D. Winge, D. Eide, A. Bird, 2006, Journal of Biological Chemistry.

Metal-specific synthesis of two metallothioneins and gamma-glutamyl peptides in Candida glabrata.

R. Mehra, D. Winge, W. Gray, 1988, Proceedings of the National Academy of Sciences of the United States of America.

Separation of three mouse metallothionein isoforms by free-solution capillary electrophoresis.

D. Winge, M. Richards, G. Andrews, 1996, Journal of chromatography. B, Biomedical applications.

Studies on the gamma-glutamyl Cu-binding peptide from Schizosaccharomyces pombe.

R. Mehra, R. Reese, D. Winge, 1988, The Journal of biological chemistry.

Oligomerization of Heme o Synthase in Cytochrome Oxidase Biogenesis Is Mediated by Cytochrome Oxidase Assembly Factor Coa2*

D. Winge, O. Khalimonchuk, X. Pérez-Martínez, 2012, The Journal of Biological Chemistry.

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.

Normal Physiology of Copper Metabolism

D. Winge, 1984, Seminars in liver disease.

Analysis of SDHAF3 in familial and sporadic pheochromocytoma and paraganglioma

T. Dwight, D. Winge, A. Gill, 2017, BMC Cancer.

The growth inhibitory activity of metallothionein-3 correlates with its novel β domain sequence rather than metal binding properties

R. Palmiter, D. Winge, L. T. Jensen, 1999 .

Identification of a DNA-binding site for the transcription factor Haa1, required for Saccharomyces cerevisiae response to acetic acid stress

Miguel C. Teixeira, D. Winge, C. Arraiano, 2011, Nucleic acids research.

The Human Cytochrome c Oxidase Assembly Factors SCO1 and SCO2 Have Regulatory Roles in the Maintenan

E. Shoubridge, P. Rustin, D. Winge, 2007 .

The Cu-Thiolate Cluster in Mutants of Yeast Metallothionein

D. Winge, 1988 .

Metal thiolate coordination in the E7 proteins of human papilloma virus 16 and cottontail rabbit papilloma virus as expressed in Escherichia coli.

D. Winge, C. Dameron, D. Smotkin, 1992, Journal of Biological Chemistry.

SDH5, a Gene Required for Flavination of Succinate Dehydrogenase, Is Mutated in Paraganglioma

S. Gygi, C. Cremers, P. Devilee, 2009, Science.

Inner Secrets of the Respirasome

D. Winge, A. Melber, 2016, Cell.

The metallothionein structural motif in gene expression.

D. Winge, G. George, C. Dameron, 1994, Advances in inorganic biochemistry.

Iron-Mediated Inhibition of Mitochondrial Manganese Uptake Mediates Mitochondrial Dysfunction in a Mouse Model of Hemochromatosis

D. Winge, E. Abel, S. Boudina, 2008, Molecular medicine.

The structure of mammalian hexokinase-1

M. Posewitz, M. Summers, D. Winge, 1998, Nature Structural Biology.

"Pulling the plug" on cellular copper: the role of mitochondria in copper export.

D. Winge, P. Cobine, S. Leary, 2009, Biochimica et biophysica acta.

Calcium, magnesium and the conformation of parvalbumin during muscular activity.

J. Cox, D. Winge, E. A. Stein, 1979, Biochimie.

Pet191 Is a Cytochrome c Oxidase Assembly Factor in Saccharomyces cerevisiae

D. Winge, P. Cobine, O. Khalimonchuk, 2008, Eukaryotic Cell.

Specific Copper Transfer from the Cox17 Metallochaperone to Both Sco1 and Cox11 in the Assembly of Yeast Cytochrome c Oxidase*

D. Winge, P. Cobine, H. Carr, 2004, Journal of Biological Chemistry.