| Year |
Citation |
Score |
| 2020 |
Nowinski SM, Solmonson A, Rusin SF, Maschek JA, Bensard CL, Fogarty S, Jeong MY, Lettlova S, Berg JA, Morgan JT, Ouyang Y, Naylor BC, Paulo JA, Funai K, Cox JE, ... ... Winge DR, et al. Mitochondrial fatty acid synthesis coordinates oxidative metabolism in mammalian mitochondria. Elife. 9. PMID 32804083 DOI: 10.7554/Elife.58041 |
0.339 |
|
| 2020 |
Hughes CE, Coody TK, Jeong MY, Berg JA, Winge DR, Hughes AL. Cysteine Toxicity Drives Age-Related Mitochondrial Decline by Altering Iron Homeostasis. Cell. 180: 296-310.e18. PMID 31978346 DOI: 10.1016/J.Cell.2019.12.035 |
0.365 |
|
| 2020 |
Nowinski SM, Solmonson A, Rusin SF, Maschek JA, Bensard CL, Fogarty S, Jeong M, Lettlova S, Berg JA, Morgan JT, Ouyang Y, Naylor BC, Paulo JA, Funai K, Cox JE, ... ... Winge DR, et al. Author response: Mitochondrial fatty acid synthesis coordinates oxidative metabolism in mammalian mitochondria Elife. DOI: 10.7554/Elife.58041.Sa2 |
0.307 |
|
| 2018 |
Chun H, Korolnek T, Lee CJ, Coyne HJ, Winge DR, Kim BE, Petris MJ. An extracellular histidine-containing motif in the zinc transporter ZIP4 plays a role in zinc sensing and zinc-induced endocytosis in mammalian cells. The Journal of Biological Chemistry. PMID 30593504 DOI: 10.1074/Jbc.Ra118.005203 |
0.397 |
|
| 2018 |
Van Vranken JG, Nowinski SM, Clowers KJ, Jeong MY, Ouyang Y, Berg JA, Gygi JP, Gygi SP, Winge DR, Rutter J. ACP Acylation Is an Acetyl-CoA-Dependent Modification Required for Electron Transport Chain Assembly. Molecular Cell. 71: 567-580.e4. PMID 30118679 DOI: 10.1016/J.Molcel.2018.06.039 |
0.341 |
|
| 2018 |
Braymer JJ, Winge DR. Sulfur from Within: Cytosolic tRNA Thiouridinylation. Cell Chemical Biology. 25: 645-647. PMID 29932897 DOI: 10.1016/J.Chembiol.2018.06.003 |
0.316 |
|
| 2018 |
Melber A, Winge DR. Steps Toward Understanding Mitochondrial Fe/S Cluster Biogenesis. Methods in Enzymology. 599: 265-292. PMID 29746243 DOI: 10.1016/Bs.Mie.2017.09.004 |
0.326 |
|
| 2018 |
García-Guerrero AE, Camacho-Villasana Y, Zamudio-Ochoa A, Winge DR, Pérez-Martínez X. Cbp3 and Cbp6 are dispensable for synthesis regulation of Cytochromein yeast mitochondria. The Journal of Biological Chemistry. PMID 29475949 DOI: 10.1074/Jbc.Ra117.000547 |
0.378 |
|
| 2018 |
Winge DR. Filling the mitochondrial copper pool. The Journal of Biological Chemistry. 293: 1897-1898. PMID 29462794 DOI: 10.1074/Jbc.H118.001457 |
0.473 |
|
| 2017 |
Sommakia S, Houlihan PR, Deane SS, Simcox JA, Torres NS, Jeong MY, Winge DR, Villanueva CJ, Chaudhuri D. Mitochondrial cardiomyopathies feature increased uptake and diminished efflux of mitochondrial calcium. Journal of Molecular and Cellular Cardiology. PMID 28962857 DOI: 10.1016/J.Yjmcc.2017.09.009 |
0.301 |
|
| 2017 |
M Fetherolf M, Boyd SD, Winkler DD, Winge DR. Oxygen-dependent activation of Cu,Zn-superoxide dismutase-1. Metallomics : Integrated Biometal Science. PMID 28686251 DOI: 10.1039/C6Mt00298F |
0.413 |
|
| 2017 |
Cory SA, Van Vranken JG, Brignole EJ, Patra S, Winge DR, Drennan CL, Rutter J, Barondeau DP. Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. Proceedings of the National Academy of Sciences of the United States of America. PMID 28634302 DOI: 10.1073/Pnas.1702849114 |
0.363 |
|
| 2017 |
Fetherolf MM, Boyd SD, Taylor AB, Kim HJ, Wohlschlegel JA, Blackburn NJ, Hart PJ, Winge DR, Winkler DD. Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper-ion entry site. The Journal of Biological Chemistry. PMID 28533431 DOI: 10.1074/Jbc.M117.775981 |
0.458 |
|
| 2016 |
Dela Cruz R, Jeong MY, Winge DR. Cox1 mutation abrogates need for Cox23 in cytochrome c oxidase biogenesis. Microbial Cell (Graz, Austria). 3: 275-284. PMID 28357365 DOI: 10.15698/Mic2016.07.511 |
0.359 |
|
| 2016 |
Van Vranken JG, Jeong MY, Wei P, Chen YC, Gygi SP, Winge DR, Rutter J. The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis. Elife. 5. PMID 27540631 DOI: 10.7554/Elife.17828 |
0.378 |
|
| 2016 |
Melber A, Na U, Vashisht A, Weiler BD, Lill R, Wohlschlegel JA, Winge DR. Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients. Elife. 5. PMID 27532773 DOI: 10.7554/Elife.15991 |
0.347 |
|
| 2016 |
Kim H, Jeong MY, Parnell TJ, Babst M, Phillips JD, Winge DR. The Plasma Membrane Protein Nce102 Implicated in Eisosome Formation Rescues A Heme Defect in Mitochondria. The Journal of Biological Chemistry. PMID 27317660 DOI: 10.1074/Jbc.M116.727743 |
0.384 |
|
| 2016 |
Vranken JGV, Jeong M, Wei P, Chen Y, Gygi SP, Winge DR, Rutter J. Author response: The mitochondrial acyl carrier protein (ACP) coordinates mitochondrial fatty acid synthesis with iron sulfur cluster biogenesis Elife. DOI: 10.7554/Elife.17828.019 |
0.387 |
|
| 2016 |
Melber A, Na U, Vashisht A, Weiler BD, Lill R, Wohlschlegel JA, Winge DR. Author response: Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients Elife. DOI: 10.7554/Elife.15991.018 |
0.35 |
|
| 2015 |
Van Vranken JG, Na U, Winge DR, Rutter J. Protein-mediated assembly of succinate dehydrogenase and its cofactors. Critical Reviews in Biochemistry and Molecular Biology. 50: 168-80. PMID 25488574 DOI: 10.3109/10409238.2014.990556 |
0.336 |
|
| 2014 |
Na U, Yu W, Cox J, Bricker DK, Brockmann K, Rutter J, Thummel CS, Winge DR. The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur subunit of succinate dehydrogenase. Cell Metabolism. 20: 253-66. PMID 24954417 DOI: 10.1016/J.Cmet.2014.05.014 |
0.375 |
|
| 2014 |
Cui TZ, Conte A, Fox JL, Zara V, Winge DR. Modulation of the respiratory supercomplexes in yeast: enhanced formation of cytochrome oxidase increases the stability and abundance of respiratory supercomplexes. The Journal of Biological Chemistry. 289: 6133-41. PMID 24421313 DOI: 10.1074/Jbc.M113.523688 |
0.319 |
|
| 2013 |
Vest KE, Leary SC, Winge DR, Cobine PA. Copper import into the mitochondrial matrix in Saccharomyces cerevisiae is mediated by Pic2, a mitochondrial carrier family protein. The Journal of Biological Chemistry. 288: 23884-92. PMID 23846699 DOI: 10.1074/Jbc.M113.470674 |
0.478 |
|
| 2013 |
Leary SC, Cobine PA, Nishimura T, Verdijk RM, de Krijger R, de Coo R, Tarnopolsky MA, Winge DR, Shoubridge EA. COX19 mediates the transduction of a mitochondrial redox signal from SCO1 that regulates ATP7A-mediated cellular copper efflux. Molecular Biology of the Cell. 24: 683-91. PMID 23345593 DOI: 10.1091/Mbc.E12-09-0705 |
0.502 |
|
| 2013 |
Patil VA, Fox JL, Gohil VM, Winge DR, Greenberg ML. Loss of cardiolipin leads to perturbation of mitochondrial and cellular iron homeostasis. The Journal of Biological Chemistry. 288: 1696-705. PMID 23192348 DOI: 10.1074/Jbc.M112.428938 |
0.379 |
|
| 2013 |
Sánchez E, Lobo T, Fox JL, Zeviani M, Winge DR, Fernández-Vizarra E. LYRM7/MZM1L is a UQCRFS1 chaperone involved in the last steps of mitochondrial Complex III assembly in human cells. Biochimica Et Biophysica Acta. 1827: 285-93. PMID 23168492 DOI: 10.1016/J.Bbabio.2012.11.003 |
0.396 |
|
| 2012 |
Eletsky A, Jeong MY, Kim H, Lee HW, Xiao R, Pagliarini DJ, Prestegard JH, Winge DR, Montelione GT, Szyperski T. Solution NMR structure of yeast succinate dehydrogenase flavinylation factor Sdh5 reveals a putative Sdh1 binding site. Biochemistry. 51: 8475-7. PMID 23062074 DOI: 10.1021/Bi301171U |
0.371 |
|
| 2012 |
Kim HJ, Jeong MY, Na U, Winge DR. Flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunit. The Journal of Biological Chemistry. 287: 40670-9. PMID 23043141 DOI: 10.1074/Jbc.M112.405704 |
0.338 |
|
| 2012 |
Cui TZ, Smith PM, Fox JL, Khalimonchuk O, Winge DR. Late-stage maturation of the Rieske Fe/S protein: Mzm1 stabilizes Rip1 but does not facilitate its translocation by the AAA ATPase Bcs1. Molecular and Cellular Biology. 32: 4400-9. PMID 22927643 DOI: 10.1128/Mcb.00441-12 |
0.383 |
|
| 2012 |
Khalimonchuk O, Kim H, Watts T, Perez-Martinez X, Winge DR. Oligomerization of heme o synthase in cytochrome oxidase biogenesis is mediated by cytochrome oxidase assembly factor Coa2. The Journal of Biological Chemistry. 287: 26715-26. PMID 22669974 DOI: 10.1074/Jbc.M112.377200 |
0.382 |
|
| 2012 |
Winge DR. Sealing the mitochondrial respirasome. Molecular and Cellular Biology. 32: 2647-52. PMID 22586278 DOI: 10.1128/Mcb.00573-12 |
0.329 |
|
| 2012 |
Smith PM, Fox JL, Winge DR. Reprint of: Biogenesis of the cytochrome bc(1) complex and role of assembly factors. Biochimica Et Biophysica Acta. 1817: 872-82. PMID 22564912 DOI: 10.1016/J.Bbabio.2012.03.003 |
0.343 |
|
| 2012 |
Kim HJ, Khalimonchuk O, Smith PM, Winge DR. Structure, function, and assembly of heme centers in mitochondrial respiratory complexes. Biochimica Et Biophysica Acta. 1823: 1604-16. PMID 22554985 DOI: 10.1016/J.Bbamcr.2012.04.008 |
0.397 |
|
| 2012 |
Turski ML, Brady DC, Kim HJ, Kim BE, Nose Y, Counter CM, Winge DR, Thiele DJ. A novel role for copper in Ras/mitogen-activated protein kinase signaling. Molecular and Cellular Biology. 32: 1284-95. PMID 22290441 DOI: 10.1128/Mcb.05722-11 |
0.397 |
|
| 2012 |
Khalimonchuk O, Jeong MY, Watts T, Ferris E, Winge DR. Selective Oma1 protease-mediated proteolysis of Cox1 subunit of cytochrome oxidase in assembly mutants. The Journal of Biological Chemistry. 287: 7289-300. PMID 22219186 DOI: 10.1074/Jbc.M111.313148 |
0.368 |
|
| 2012 |
Smith PM, Fox JL, Winge DR. Biogenesis of the cytochrome bc(1) complex and role of assembly factors. Biochimica Et Biophysica Acta. 1817: 276-86. PMID 22138626 DOI: 10.1016/J.Bbabio.2011.11.009 |
0.343 |
|
| 2011 |
Atkinson A, Smith P, Fox JL, Cui TZ, Khalimonchuk O, Winge DR. The LYR protein Mzm1 functions in the insertion of the Rieske Fe/S protein in yeast mitochondria. Molecular and Cellular Biology. 31: 3988-96. PMID 21807901 DOI: 10.1128/Mcb.05673-11 |
0.384 |
|
| 2011 |
Frey AG, Bird AJ, Evans-Galea MV, Blankman E, Winge DR, Eide DJ. Zinc-regulated DNA binding of the yeast Zap1 zinc-responsive activator. Plos One. 6: e22535. PMID 21799889 DOI: 10.1371/Journal.Pone.0022535 |
0.372 |
|
| 2011 |
Dodani SC, Leary SC, Cobine PA, Winge DR, Chang CJ. A targetable fluorescent sensor reveals that copper-deficient SCO1 and SCO2 patient cells prioritize mitochondrial copper homeostasis. Journal of the American Chemical Society. 133: 8606-16. PMID 21563821 DOI: 10.1021/Ja2004158 |
0.482 |
|
| 2011 |
Watts T, Khalimonchuk O, Wolf RZ, Turk EM, Mohr G, Winge DR. Mne1 is a novel component of the mitochondrial splicing apparatus responsible for processing of a COX1 group I intron in yeast. The Journal of Biological Chemistry. 286: 10137-46. PMID 21257754 DOI: 10.1074/Jbc.M110.205625 |
0.384 |
|
| 2011 |
Li H, Mapolelo DT, Dingra NN, Keller G, Riggs-Gelasco PJ, Winge DR, Johnson MK, Outten CE. 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 Journal of Biological Chemistry. 286: 867-76. PMID 20978135 DOI: 10.1074/Jbc.M110.184176 |
0.342 |
|
| 2010 |
Bestwick M, Jeong MY, Khalimonchuk O, Kim H, Winge DR. Analysis of Leigh syndrome mutations in the yeast SURF1 homolog reveals a new member of the cytochrome oxidase assembly factor family. Molecular and Cellular Biology. 30: 4480-91. PMID 20624914 DOI: 10.1128/Mcb.00228-10 |
0.401 |
|
| 2010 |
Thompson AK, Smith D, Gray J, Carr HS, Liu A, Winge DR, Hosler JP. Mutagenic analysis of Cox11 of Rhodobacter sphaeroides: insights into the assembly of Cu(B) of cytochrome c oxidase. Biochemistry. 49: 5651-61. PMID 20524628 DOI: 10.1021/Bi1003876 |
0.504 |
|
| 2010 |
Atkinson A, Khalimonchuk O, Smith P, Sabic H, Eide D, Winge DR. Mzm1 influences a labile pool of mitochondrial zinc important for respiratory function. The Journal of Biological Chemistry. 285: 19450-9. PMID 20404342 DOI: 10.1074/Jbc.M110.109793 |
0.453 |
|
| 2010 |
Rutter J, Winge DR, Schiffman JD. Succinate dehydrogenase - Assembly, regulation and role in human disease. Mitochondrion. 10: 393-401. PMID 20226277 DOI: 10.1016/J.Mito.2010.03.001 |
0.319 |
|
| 2010 |
Robinson NJ, Winge DR. Copper metallochaperones. Annual Review of Biochemistry. 79: 537-62. PMID 20205585 DOI: 10.1146/annurev-biochem-030409-143539 |
0.388 |
|
| 2010 |
Khalimonchuk O, Bestwick M, Meunier B, Watts TC, Winge DR. Formation of the redox cofactor centers during Cox1 maturation in yeast cytochrome oxidase. Molecular and Cellular Biology. 30: 1004-17. PMID 19995914 DOI: 10.1128/Mcb.00640-09 |
0.439 |
|
| 2010 |
Bestwick M, Khalimonchuk O, Pierrel F, Winge DR. The role of Coa2 in hemylation of yeast Cox1 revealed by its genetic interaction with Cox10 Molecular and Cellular Biology. 30: 172-185. PMID 19841065 DOI: 10.1128/Mcb.00869-09 |
0.389 |
|
| 2009 |
Shaw JM, Winge DR. Shaping the mitochondrion: mitochondrial biogenesis, dynamics and dysfunction. Conference on Mitochondrial Assembly and Dynamics in Health and Disease. Embo Reports. 10: 1301-5. PMID 19949411 DOI: 10.1038/Embor.2009.247 |
0.365 |
|
| 2009 |
Wu CY, Roje S, Sandoval FJ, Bird AJ, Winge DR, Eide DJ. Repression of sulfate assimilation is an adaptive response of yeast to the oxidative stress of zinc deficiency. The Journal of Biological Chemistry. 284: 27544-56. PMID 19656949 DOI: 10.1074/Jbc.M109.042036 |
0.334 |
|
| 2009 |
Hao HX, Khalimonchuk O, Schraders M, Dephoure N, Bayley JP, Kunst H, Devilee P, Cremers CW, Schiffman JD, Bentz BG, Gygi SP, Winge DR, Kremer H, Rutter J. SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma. Science (New York, N.Y.). 325: 1139-42. PMID 19628817 DOI: 10.1126/Science.1175689 |
0.364 |
|
| 2009 |
Atkinson A, Winge DR. Metal acquisition and availability in the mitochondria. Chemical Reviews. 109: 4708-21. PMID 19522505 DOI: 10.1021/Cr900006Y |
0.35 |
|
| 2009 |
Winge DR, Tzagoloff A. Assembly of the Mitochondrial Respiratory Chain Biochimica Et Biophysica Acta - Molecular Cell Research. 1793: 1. PMID 19028255 DOI: 10.1016/J.Bbamcr.2008.11.002 |
0.314 |
|
| 2009 |
Leary SC, Winge DR, Cobine PA. "Pulling the plug" on cellular copper: the role of mitochondria in copper export. Biochimica Et Biophysica Acta. 1793: 146-53. PMID 18522804 DOI: 10.1016/J.Bbamcr.2008.05.002 |
0.505 |
|
| 2008 |
Zhang L, Pickering IJ, Winge DR, George GN. X-ray absorption spectroscopy of cuprous-thiolate clusters in Saccharomyces cerevisiae metallothionein. Chemistry & Biodiversity. 5: 2042-9. PMID 18972536 DOI: 10.1002/Cbdv.200890186 |
0.457 |
|
| 2008 |
Wu CY, Bird AJ, Chung LM, Newton MA, Winge DR, Eide DJ. Differential control of Zap1-regulated genes in response to zinc deficiency in Saccharomyces cerevisiae. Bmc Genomics. 9: 370. PMID 18673560 DOI: 10.1186/1471-2164-9-370 |
0.323 |
|
| 2008 |
Pierrel F, Khalimonchuk O, Cobine PA, Bestwick M, Winge DR. Coa2 is an assembly factor for yeast cytochrome c oxidase biogenesis that facilitates the maturation of Cox1 Molecular and Cellular Biology. 28: 4927-4939. PMID 18541668 DOI: 10.1128/Mcb.00057-08 |
0.405 |
|
| 2008 |
Khalimonchuk O, Rigby K, Bestwick M, Pierrel F, Cobine PA, Winge DR. Pet191 is a cytochrome c oxidase assembly factor in Saccharomyces cerevisiae Eukaryotic Cell. 7: 1427-1431. PMID 18503002 DOI: 10.1128/Ec.00132-08 |
0.371 |
|
| 2008 |
Rigby K, Cobine PA, Khalimonchuk O, Winge DR. Mapping the functional interaction of Sco1 and Cox2 in cytochrome oxidase biogenesis. The Journal of Biological Chemistry. 283: 15015-22. PMID 18390903 DOI: 10.1074/Jbc.M710072200 |
0.475 |
|
| 2008 |
Jouihan HA, Cobine PA, Cooksey RC, Hoagland EA, Boudina S, Abel ED, Winge DR, McClain DA. Iron-mediated inhibition of mitochondrial manganese uptake mediates mitochondrial dysfunction in a mouse model of hemochromatosis. Molecular Medicine (Cambridge, Mass.). 14: 98-108. PMID 18317567 DOI: 10.2119/2007-00114.Jouihan |
0.407 |
|
| 2008 |
Kumánovics A, Chen OS, Li L, Bagley D, Adkins EM, Lin H, Dingra NN, Outten CE, Keller G, Winge D, Ward DM, Kaplan J. Identification of FRA1 and FRA2 as genes involved in regulating the yeast iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis. The Journal of Biological Chemistry. 283: 10276-86. PMID 18281282 DOI: 10.1074/Jbc.M801160200 |
0.388 |
|
| 2008 |
Khalimonchuk O, Winge DR. Function and redox state of mitochondrial localized cysteine-rich proteins important in the assembly of cytochrome c oxidase. Biochimica Et Biophysica Acta. 1783: 618-28. PMID 18070608 DOI: 10.1016/J.Bbamcr.2007.10.016 |
0.418 |
|
| 2007 |
Pierrel F, Bestwick ML, Cobine PA, Khalimonchuk O, Cricco JA, Winge DR. Coa1 links the Mss51 post-translational function to Cox1 cofactor insertion in cytochrome c oxidase assembly Embo Journal. 26: 4335-4346. PMID 17882260 DOI: 10.1038/Sj.Emboj.7601861 |
0.472 |
|
| 2007 |
Khalimonchuk O, Bird A, Winge DR. Evidence for a pro-oxidant intermediate in the assembly of cytochrome oxidase. The Journal of Biological Chemistry. 282: 17442-9. PMID 17430883 DOI: 10.1074/Jbc.M702379200 |
0.422 |
|
| 2007 |
Leary SC, Winge DR. The Janus face of copper: its expanding roles in biology and the pathophysiology of disease. Meeting on Copper and Related Metals in Biology. Embo Reports. 8: 224-7. PMID 17304237 DOI: 10.1038/Sj.Embor.7400915 |
0.474 |
|
| 2007 |
Rigby K, Zhang L, Cobine PA, George GN, Winge DR. characterization of the cytochrome c oxidase assembly factor Cox19 of Saccharomyces cerevisiae. The Journal of Biological Chemistry. 282: 10233-42. PMID 17237235 DOI: 10.1074/Jbc.M610082200 |
0.531 |
|
| 2007 |
Pierrel F, Cobine PA, Winge DR. Metal Ion availability in mitochondria Biometals. 20: 675-682. PMID 17225062 DOI: 10.1007/S10534-006-9052-9 |
0.353 |
|
| 2007 |
Coyne HJ, Ciofi-Baffoni S, Banci L, Bertini I, Zhang L, George GN, Winge DR. The characterization and role of zinc binding in yeast Cox4. The Journal of Biological Chemistry. 282: 8926-34. PMID 17215247 DOI: 10.1074/Jbc.M610303200 |
0.46 |
|
| 2007 |
Leary SC, Cobine PA, Kaufman BA, Guercin GH, Mattman A, Palaty J, Lockitch G, Winge DR, Rustin P, Horvath R, Shoubridge EA. The human cytochrome c oxidase assembly factors SCO1 and SCO2 have regulatory roles in the maintenance of cellular copper homeostasis. Cell Metabolism. 5: 9-20. PMID 17189203 DOI: 10.1016/J.Cmet.2006.12.001 |
0.5 |
|
| 2007 |
Wu CY, Bird AJ, Winge DR, Eide DJ. Regulation of the yeast TSA1 peroxiredoxin by ZAP1 is an adaptive response to the oxidative stress of zinc deficiency. The Journal of Biological Chemistry. 282: 2184-95. PMID 17121842 DOI: 10.1074/Jbc.M606639200 |
0.346 |
|
| 2007 |
Leary SC, Cobine PA, Kaufman BA, Guercin GH, Mattman A, Palaty J, Lockitch G, Winge DR, Rustin P, Horvath R, Shoubridge EA. The Human Cytochrome c Oxidase Assembly Factors SCO1 and SCO2 Have Regulatory Roles in the Maintenance of Cellular Copper Homeostasis (DOI:10.1016/j.cmet.2006.12.001) Cell Metabolism. 5: 403. DOI: 10.1016/J.Cmet.2007.04.002 |
0.401 |
|
| 2006 |
Bird AJ, Gordon M, Eide DJ, Winge DR. Repression of ADH1 and ADH3 during zinc deficiency by Zap1-induced intergenic RNA transcripts. The Embo Journal. 25: 5726-34. PMID 17139254 DOI: 10.1038/Sj.Emboj.7601453 |
0.356 |
|
| 2006 |
Cobine PA, Pierrel F, Bestwick ML, Winge DR. Mitochondrial matrix copper complex used in metallation of cytochrome oxidase and superoxide dismutase Journal of Biological Chemistry. 281: 36552-36559. PMID 17008312 DOI: 10.1074/Jbc.M606839200 |
0.489 |
|
| 2006 |
Bird AJ, Swierczek S, Qiao W, Eide DJ, Winge DR. Zinc metalloregulation of the zinc finger pair domain. The Journal of Biological Chemistry. 281: 25326-35. PMID 16829533 DOI: 10.1074/Jbc.M600655200 |
0.386 |
|
| 2006 |
Cobine PA, Winge DR. Visualizing tricoordinate copper transfer. Nature Chemical Biology. 2: 352-3. PMID 16783337 DOI: 10.1038/Nchembio0706-352 |
0.451 |
|
| 2006 |
Qiao W, Mooney M, Bird AJ, Winge DR, Eide DJ. Zinc binding to a regulatory zinc-sensing domain monitored in vivo by using FRET. Proceedings of the National Academy of Sciences of the United States of America. 103: 8674-9. PMID 16720702 DOI: 10.1073/Pnas.0600928103 |
0.377 |
|
| 2006 |
Ojeda L, Keller G, Muhlenhoff U, Rutherford JC, Lill R, Winge DR. Role of glutaredoxin-3 and glutaredoxin-4 in the iron regulation of the Aft1 transcriptional activator in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 281: 17661-9. PMID 16648636 DOI: 10.1074/Jbc.M602165200 |
0.767 |
|
| 2006 |
Cobine PA, Pierrel F, Winge DR. Copper trafficking to the mitochondrion and assembly of copper metalloenzymes Biochimica Et Biophysica Acta - Molecular Cell Research. 1763: 759-772. PMID 16631971 DOI: 10.1016/J.Bbamcr.2006.03.002 |
0.514 |
|
| 2006 |
Yang M, Cobine PA, Molik S, Naranuntarat A, Lill R, Winge DR, Culotta VC. The effects of mitochondrial iron homeostasis on cofactor specificity of superoxide dismutase 2. The Embo Journal. 25: 1775-83. PMID 16601688 DOI: 10.1038/Sj.Emboj.7601064 |
0.411 |
|
| 2006 |
Cobine PA, Pierrel F, Leary SC, Sasarman F, Horng YC, Shoubridge EA, Winge DR. The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding Journal of Biological Chemistry. 281: 12270-12276. PMID 16520371 DOI: 10.1074/Jbc.M600496200 |
0.533 |
|
| 2005 |
Keller G, Bird A, Winge DR. Independent metalloregulation of Ace1 and Mac1 in Saccharomyces cerevisiae. Eukaryotic Cell. 4: 1863-71. PMID 16278453 DOI: 10.1128/Ec.4.11.1863-1871.2005 |
0.474 |
|
| 2005 |
Horng YC, Leary SC, Cobine PA, Young FB, George GN, Shoubridge EA, Winge DR. Human Sco1 and Sco2 function as copper-binding proteins. The Journal of Biological Chemistry. 280: 34113-22. PMID 16091356 DOI: 10.1074/Jbc.M506801200 |
0.474 |
|
| 2005 |
Herbig A, Bird AJ, Swierczek S, McCall K, Mooney M, Wu CY, Winge DR, Eide DJ. Zap1 activation domain 1 and its role in controlling gene expression in response to cellular zinc status. Molecular Microbiology. 57: 834-46. PMID 16045625 DOI: 10.1111/J.1365-2958.2005.04734.X |
0.351 |
|
| 2005 |
Arnesano F, Balatri E, Banci L, Bertini I, Winge DR. Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding. Structure (London, England : 1993). 13: 713-22. PMID 15893662 DOI: 10.1016/J.Str.2005.02.015 |
0.496 |
|
| 2005 |
Carr HS, Maxfield AB, Horng YC, Winge DR. Functional analysis of the domains in Cox11. The Journal of Biological Chemistry. 280: 22664-9. PMID 15840584 DOI: 10.1074/Jbc.M414077200 |
0.497 |
|
| 2005 |
Rutherford JC, Ojeda L, Balk J, Mühlenhoff U, Lill R, Winge DR. Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis. The Journal of Biological Chemistry. 280: 10135-40. PMID 15649888 DOI: 10.1074/Jbc.M413731200 |
0.77 |
|
| 2004 |
Horng YC, Cobine PA, Maxfield AB, Carr HS, Winge DR. Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase. The Journal of Biological Chemistry. 279: 35334-40. PMID 15199057 DOI: 10.1074/Jbc.M404747200 |
0.496 |
|
| 2004 |
Chen OS, Crisp RJ, Valachovic M, Bard M, Winge DR, Kaplan J. Transcription of the yeast iron regulon does not respond directly to iron but rather to iron-sulfur cluster biosynthesis. The Journal of Biological Chemistry. 279: 29513-8. PMID 15123701 DOI: 10.1074/Jbc.M403209200 |
0.356 |
|
| 2004 |
Bird AJ, Blankman E, Stillman DJ, Eide DJ, Winge DR. The Zap1 transcriptional activator also acts as a repressor by binding downstream of the TATA box in ZRT2. The Embo Journal. 23: 1123-32. PMID 14976557 DOI: 10.1038/Sj.Emboj.7600122 |
0.351 |
|
| 2004 |
Cobine PA, Ojeda LD, Rigby KM, Winge DR. Yeast contain a non-proteinaceous pool of copper in the mitochondrial matrix. The Journal of Biological Chemistry. 279: 14447-55. PMID 14729672 DOI: 10.1074/Jbc.M312693200 |
0.801 |
|
| 2004 |
Maxfield AB, Heaton DN, Winge DR. Cox17 is functional when tethered to the mitochondrial inner membrane. The Journal of Biological Chemistry. 279: 5072-80. PMID 14615477 DOI: 10.1074/Jbc.M311772200 |
0.784 |
|
| 2003 |
Winge DR. Let's Sco1, Oxidase! Let's Sco! Structure (London, England : 1993). 11: 1313-4. PMID 14604519 DOI: 10.1016/J.Str.2003.10.006 |
0.409 |
|
| 2003 |
Bird AJ, McCall K, Kramer M, Blankman E, Winge DR, Eide DJ. Zinc fingers can act as Zn2+ sensors to regulate transcriptional activation domain function. The Embo Journal. 22: 5137-46. PMID 14517251 DOI: 10.1093/Emboj/Cdg484 |
0.364 |
|
| 2003 |
Rutherford JC, Jaron S, Winge DR. Aft1p and Aft2p mediate iron-responsive gene expression in yeast through related promoter elements. The Journal of Biological Chemistry. 278: 27636-43. PMID 12756250 DOI: 10.1074/Jbc.M300076200 |
0.335 |
|
| 2003 |
Carr HS, Winge DR. Assembly of cytochrome c oxidase within the mitochondrion. Accounts of Chemical Research. 36: 309-16. PMID 12755640 DOI: 10.1021/Ar0200807 |
0.451 |
|
| 2003 |
Evans-Galea MV, Blankman E, Myszka DG, Bird AJ, Eide DJ, Winge DR. Two of the five zinc fingers in the Zap1 transcription factor DNA binding domain dominate site-specific DNA binding Biochemistry. 42: 1053-1061. PMID 12549926 DOI: 10.1021/Bi0263199 |
0.365 |
|
| 2003 |
Winge DR, Maxfield A, Carr H, Cobine P, McCall K. Proteins involved in the metallation of copper centers in cytochrome c oxidase Journal of Inorganic Biochemistry. 96: 45. DOI: 10.1016/S0162-0134(03)80481-6 |
0.413 |
|
| 2002 |
Winge DR. Copper metalloregulation of gene expression. Advances in Protein Chemistry. 60: 51-92. PMID 12418175 DOI: 10.1016/S0065-3233(02)60051-8 |
0.478 |
|
| 2002 |
Daniels PJ, Bittel D, Smirnova IV, Winge DR, Andrews GK. 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. Nucleic Acids Research. 30: 3130-40. PMID 12136095 DOI: 10.1093/Nar/Gkf432 |
0.374 |
|
| 2002 |
Romero-Isart N, Jensen LT, Zerbe O, Winge DR, Vasak M. Engineering of metallothionein-3 neuroinhibitory activity into the inactive isoform metallothionein-1. The Journal of Biological Chemistry. 277: 37023-8. PMID 12130647 DOI: 10.1074/Jbc.M205730200 |
0.314 |
|
| 2002 |
Carr HS, George GN, Winge DR. Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein. The Journal of Biological Chemistry. 277: 31237-42. PMID 12063264 DOI: 10.1074/Jbc.M204854200 |
0.529 |
|
| 2002 |
Brown KR, Keller GL, Pickering IJ, Harris HH, George GN, Winge DR. Structures of the cuprous-thiolate clusters of the Mac1 and Ace1 transcriptional activators. Biochemistry. 41: 6469-76. PMID 12009910 DOI: 10.1021/Bi0160664 |
0.478 |
|
| 2001 |
Rutherford JC, Jaron S, Ray E, Brown PO, Winge DR. A second iron-regulatory system in yeast independent of Aft1p. Proceedings of the National Academy of Sciences of the United States of America. 98: 14322-7. PMID 11734641 DOI: 10.1073/Pnas.261381198 |
0.353 |
|
| 2001 |
Nittis T, George GN, Winge DR. Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein. The Journal of Biological Chemistry. 276: 42520-6. PMID 11546815 DOI: 10.1074/Jbc.M107077200 |
0.819 |
|
| 2001 |
Keller G, Ray E, Brown PO, Winge DR. Haa1, a protein homologous to the copper-regulated transcription factor Ace1, is a novel transcriptional activator. The Journal of Biological Chemistry. 276: 38697-702. PMID 11504737 DOI: 10.1074/Jbc.M107131200 |
0.402 |
|
| 2001 |
Heaton DN, George GN, Garrison G, Winge DR. The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex. Biochemistry. 40: 743-51. PMID 11170391 DOI: 10.1021/Bi002315X |
0.777 |
|
| 2000 |
Hasler DW, Jensen LT, Zerbe O, Winge DR, Vasak M. 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 Biochemistry. 39: 14567-14575. PMID 11087412 DOI: 10.1021/Bi001569F |
0.301 |
|
| 2000 |
Heaton D, Nittis T, Srinivasan C, Winge DR. Mutational analysis of the mitochondrial copper metallochaperone Cox17. The Journal of Biological Chemistry. 275: 37582-7. PMID 10970896 DOI: 10.1074/Jbc.M006639200 |
0.755 |
|
| 2000 |
Gross C, Kelleher M, Iyer VR, Brown PO, Winge DR. Identification of the copper regulon in Saccharomyces cerevisiae by DNA microarrays Journal of Biological Chemistry. 275: 32310-32316. PMID 10922376 DOI: 10.1074/Jbc.M005946200 |
0.676 |
|
| 2000 |
Bird AJ, Zhao H, Luo H, Jensen LT, Srinivasan C, Evans-Galea M, Winge DR, Eide DJ. A dual role for zinc fingers in both DNA binding and zinc sensing by the Zap1 transcriptional activator. The Embo Journal. 19: 3704-13. PMID 10899124 DOI: 10.1093/Emboj/19.14.3704 |
0.405 |
|
| 2000 |
Keller G, Gross C, Kelleher M, Winge DR. Functional independence of the two cysteine-rich activation domains in the yeast Mac1 transcription factor Journal of Biological Chemistry. 275: 29193-29199. PMID 10887177 DOI: 10.1074/Jbc.M001552200 |
0.683 |
|
| 2000 |
Bird A, Evans-Galea MV, Blankman E, Zhao H, Luo H, Winge DR, Eide DJ. Mapping the DNA binding domain of the Zap1 zinc-responsive transcriptional activator Journal of Biological Chemistry. 275: 16160-16166. PMID 10747942 DOI: 10.1074/Jbc.M000664200 |
0.378 |
|
| 1999 |
Jamison McDaniels CP, Jensen LT, Srinivasan C, Winge DR, Tullius TD. The yeast transcription factor Mac1 binds to DNA in a modular fashion. The Journal of Biological Chemistry. 274: 26962-7. PMID 10480908 DOI: 10.1074/Jbc.274.38.26962 |
0.377 |
|
| 1999 |
Winge DR. Copper-regulatory domain involved in gene expression Advances in Experimental Medicine and Biology. 448: 237-246. PMID 10079831 DOI: 10.1016/S0079-6603(08)60036-7 |
0.496 |
|
| 1998 |
Jensen LT, Winge DR. Identification of a copper-induced intramolecular interaction in the transcription factor Mac1 from Saccharomyces cerevisiae Embo Journal. 17: 5400-5408. PMID 9736617 DOI: 10.1093/Emboj/17.18.5400 |
0.494 |
|
| 1998 |
Jensen LT, Posewitz MC, Srinivasan C, Winge DR. Mapping of the DNA binding domain of the copper-responsive transcription factor Mac1 from Saccharomyces cerevisiae. The Journal of Biological Chemistry. 273: 23805-11. PMID 9726991 DOI: 10.1074/Jbc.273.37.23805 |
0.415 |
|
| 1998 |
Martins LJ, Jensen LT, Simon JR, Keller GL, Winge DR, Simons JR. Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 273: 23716-21. PMID 9726978 DOI: 10.1074/Jbc.273.37.23716 |
0.448 |
|
| 1998 |
Winge DR, Jensen LT, Srinivasan C. Metal-ion regulation of gene expression in yeast. Current Opinion in Chemical Biology. 2: 216-21. PMID 9667925 DOI: 10.1016/S1367-5931(98)80063-X |
0.404 |
|
| 1998 |
Turner RB, Smith DL, Zawrotny ME, Summers MF, Posewitz MC, Winge DR. Solution structure of a zinc domain conserved in yeast copper-regulated transcription factors. Nature Structural Biology. 5: 551-5. PMID 9665167 DOI: 10.1038/805 |
0.383 |
|
| 1998 |
Srinivasan C, Posewitz MC, George GN, Winge DR. Characterization of the copper chaperone Cox17 of Saccharomyces cerevisiae. Biochemistry. 37: 7572-7. PMID 9585572 DOI: 10.1021/Bi980418Y |
0.467 |
|
| 1998 |
Jensen LT, Peltier JM, Winge DR. Identification of a four copper folding intermediate in mammalian copper metallothionein by electrospray ionization mass spectrometry Journal of Biological Inorganic Chemistry. 3: 627-631. DOI: 10.1007/S007750050276 |
0.446 |
|
| 1997 |
Graden JA, Winge DR. Copper-mediated repression of the activation domain in the yeast Mac1p transcription factor Proceedings of the National Academy of Sciences of the United States of America. 94: 5550-5555. PMID 9159110 DOI: 10.1073/Pnas.94.11.5550 |
0.497 |
|
| 1997 |
Winge DR, Graden JA, Posewitz MC, Martins LJ, Jensen LT, Simon JR. Sensors that mediate copper-specific activation and repression of gene expression Journal of Biological Inorganic Chemistry. 2: 2-10. DOI: 10.1007/S007750050100 |
0.495 |
|
| 1996 |
Graden JA, Posewitz MC, Simon JR, George GN, Pickering IJ, Winge DR. Presence of a copper(I)-thiolate regulatory domain in the copper-activated transcription factor Amt1. Biochemistry. 35: 14583-9. PMID 8931556 DOI: 10.1021/Bi961642V |
0.48 |
|
| 1996 |
Jensen LT, Howard WR, Strain JJ, Winge DR, Culotta VC. Enhanced effectiveness of copper ion buffering by CUP1 metallothionein compared with CRS5 metallothionein in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 271: 18514-9. PMID 8702498 DOI: 10.1074/Jbc.271.31.18514 |
0.488 |
|
| 1996 |
Farrell RA, Thorvaldsen JL, Winge DR. Identification of the Zn(II) site in the copper-responsive yeast transcription factor, AMT1: A conserved Zn module Biochemistry. 35: 1571-1580. PMID 8634288 DOI: 10.1021/Bi9517087 |
0.451 |
|
| 1996 |
Pérez-Alvarado GC, Kosa JL, Louis HA, Beckerle MC, Winge DR, Summers MF. Structure of the cysteine-rich intestinal protein, CRIP. Journal of Molecular Biology. 257: 153-74. PMID 8632452 DOI: 10.1006/Jmbi.1996.0153 |
0.352 |
|
| 1996 |
Yu W, Farrell RA, Stillman DJ, Winge DR. Identification of SLF1 as a new copper homeostasis gene involved in copper sulfide mineralization in Saccharomyces cerevisiae Molecular and Cellular Biology. 16: 2464-2472. PMID 8628314 DOI: 10.1128/Mcb.16.5.2464 |
0.47 |
|
| 1996 |
Posewitz MC, Simon JR, Farrell RA, Winge DR. Role of the conserved histidines in the Zn module of the copper-activated transcription factors in yeast Journal of Biological Inorganic Chemistry. 1: 560-566. DOI: 10.1007/S007750050092 |
0.446 |
|
| 1995 |
Thorvaldsen JL, Mehra RK, Yu W, Sewell AK, Winge DR. Analysis of copper-induced metallothionein expression using autonomously replicating plasmids in Candida glabrata Yeast. 11: 1501-1511. PMID 8750238 DOI: 10.1002/Yea.320111505 |
0.404 |
|
| 1995 |
Dobi A, Dameron CT, Hu S, Hamer D, Winge DR. Distinct regions of Cu(I).ACE1 contact two spatially resolved DNA major groove sites. The Journal of Biological Chemistry. 270: 10171-8. PMID 7730320 DOI: 10.1074/Jbc.270.17.10171 |
0.347 |
|
| 1995 |
Sewell AK, Jensen LT, Erickson JC, Palmiter RD, Winge DR. Bioactivity of metallothionein-3 correlates with its novel beta domain sequence rather than metal binding properties. Biochemistry. 34: 4740-7. PMID 7718580 DOI: 10.1021/Bi00014A031 |
0.371 |
|
| 1995 |
Sewell AK, Yokoya F, Yu W, Miyagawa T, Murayama T, Winge DR. Mutated yeast heat shock transcription factor exhibits elevated basal transcriptional activation and confers metal resistance Journal of Biological Chemistry. 270: 25079-25086. PMID 7559639 DOI: 10.1074/Jbc.270.42.25079 |
0.328 |
|
| 1995 |
Griffin DH, Winkelmann G, Winge DR. Metal Ions in Fungi Mycologia. 87: 425. DOI: 10.1201/9781003067221 |
0.361 |
|
| 1994 |
Kosa JL, Michelsen JW, Louis HA, Olsen JI, Davis DR, Beckerle MC, Winge DR. Common metal ion coordination in LIM domain proteins. Biochemistry. 33: 468-77. PMID 8286377 DOI: 10.1021/Bi00168A011 |
0.394 |
|
| 1994 |
Winge DR, Dameron CT, George GN. The metallothionein structural motif in gene expression Advances in Inorganic Biochemistry. 10: 1-48. PMID 8203284 |
0.385 |
|
| 1994 |
Thorvaldsen JL, Sewell AK, Tanner AM, Peltier JM, Pickering IJ, George GN, Winge DR. Mixed Cu+ and Zn2+ coordination in the DNA-binding domain of the AMT1 transcription factor from Candida glabrata. Biochemistry. 33: 9566-77. PMID 8068632 DOI: 10.1021/Bi00198A024 |
0.485 |
|
| 1994 |
Pérez-Alvarado GC, Miles C, Michelsen JW, Louis HA, Winge DR, Beckerle MC, Summers MF. Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRP. Nature Structural Biology. 1: 388-98. PMID 7664053 DOI: 10.1038/Nsb0694-388 |
0.33 |
|
| 1993 |
Michelsen JW, Schmeichel KL, Beckerle MC, Winge DR. The LIM motif defines a specific zinc-binding protein domain. Proceedings of the National Academy of Sciences of the United States of America. 90: 4404-8. PMID 8506279 DOI: 10.1073/Pnas.90.10.4404 |
0.391 |
|
| 1993 |
Winge DR. Distinct metal binding configurations in ACE Biochemistry. 32: 7294-7301. PMID 8343519 DOI: 10.1021/Bi00079A028 |
0.446 |
|
| 1993 |
Narula SS, Winge DR, Armitage IM. Copper- and silver-substituted yeast metallothioneins: sequential 1H NMR assignments reflecting conformational heterogeneity at the C terminus. Biochemistry. 32: 6773-87. PMID 8329400 DOI: 10.1021/Bi00077A032 |
0.43 |
|
| 1993 |
Pickering IJ, George GN, Dameron CT, Kurz B, Winge DR, Dance IG. X-ray absorption spectroscopy of cuprous-thiolate clusters in proteins and model systems Journal of the American Chemical Society. 115: 9498-9505. DOI: 10.1021/Ja00074A014 |
0.393 |
|
| 1993 |
Winge D, Michelsen J, Kosa J, Schmeichel K, Beckerle M. The LIM motif: A specific zinc-binding protein domain Journal of Inorganic Biochemistry. 51: 583. DOI: 10.1016/0162-0134(93)85605-8 |
0.351 |
|
| 1991 |
Dameron CT, Winge DR, George GN, Sansone M, Hu S, Hamer D. A copper-thiolate polynuclear cluster in the ACE1 transcription factor Proceedings of the National Academy of Sciences of the United States of America. 88: 6127-6131. PMID 2068093 DOI: 10.1073/Pnas.88.14.6127 |
0.465 |
|
| 1991 |
Winge DR. Copper coordination in metallothionein Methods in Enzymology. 205: 458-469. PMID 1779809 DOI: 10.1007/978-3-0348-6784-9_14 |
0.455 |
|
| 1991 |
Dameron CT, Winge DR, George GN, Hamer DH. A copper: Thiolate polynuclear cluster in the ACE1 transcription factor that mediates metallothionein gene expression Journal of Inorganic Biochemistry. 43: 127. DOI: 10.1016/0162-0134(91)84121-O |
0.358 |
|
| 1990 |
Winge DR, Mehra RK. Host defenses against copper toxicity International Review of Experimental Pathology. 31: 47-83. PMID 2292474 DOI: 10.1016/B978-0-12-364931-7.50007-0 |
0.335 |
|
| 1989 |
Brouwer M, Winge DR, Gray WR. Structural and functional diversity of copper-metallothioneins from the American lobster Homarus americanus. Journal of Inorganic Biochemistry. 35: 289-303. PMID 2709004 DOI: 10.1016/0162-0134(89)84018-8 |
0.478 |
|
| 1988 |
Mehra RK, Winge DR. Cu(I) binding to the Schizosaccharomyces pombe γ-glutamyl peptides varying in chain lengths Archives of Biochemistry and Biophysics. 265: 381-389. PMID 3421713 DOI: 10.1016/0003-9861(88)90141-5 |
0.321 |
|
| 1988 |
George GN, Byrd J, Winge DR. X-ray absorption studies of yeast copper metallothionein Journal of Biological Chemistry. 263: 8199-8203. PMID 3286647 |
0.338 |
|
| 1988 |
Thrower AR, Byrd J, Tarbet EB, Mehra RK, Hamer DH, Winge DR. Effect of mutation of cysteinyl residues in yeast Cu-metallothionein. The Journal of Biological Chemistry. 263: 7037-42. PMID 3284882 |
0.323 |
|
| 1988 |
Byrd J, Berger RM, McMillin DR, Wright CF, Hamer D, Winge DR. Characterization of the copper-thiolate cluster in yeast metallothionein and two truncated mutants. The Journal of Biological Chemistry. 263: 6688-94. PMID 3283130 |
0.345 |
|
| 1988 |
Mehra RK, Tarbet EB, Gray WR, Winge DR. Metal-specific synthesis of two metallothioneins and gamma-glutamyl peptides in Candida glabrata. Proceedings of the National Academy of Sciences of the United States of America. 85: 8815-9. PMID 3194392 DOI: 10.1073/Pnas.85.23.8815 |
0.32 |
|
| 1987 |
Furey WF, Robbins AH, Clancy LL, Winge DR, Wang BC, Stout CD. Crystal structure of Cd,Zn metallothionein Experientia. Supplementum. 52: 139-148. PMID 2959500 DOI: 10.1007/978-3-0348-6784-9_7 |
0.314 |
|
| 1986 |
Winge DR, Gray WR, Zelazowski A, Garvey JS. Sequence and antigenicity of calf metallothionein II. Archives of Biochemistry and Biophysics. 245: 254-62. PMID 3947100 DOI: 10.1016/0003-9861(86)90212-2 |
0.413 |
|
| 1986 |
Byrd J, Winge DR. Cooperative cluster formation in metallothionein Archives of Biochemistry and Biophysics. 250: 233-237. PMID 3767375 DOI: 10.1016/0003-9861(86)90721-6 |
0.435 |
|
| 1986 |
George GN, Winge D, Stout CD, Cramer SP. X-ray absorption studies of the copper-beta domain of rat liver metallothionein. Journal of Inorganic Biochemistry. 27: 213-20. PMID 3760860 DOI: 10.1016/0162-0134(86)80062-9 |
0.438 |
|
| 1985 |
Winge DR, Nielson KB, Gray WR, Hamer DH. Yeast metallothionein. Sequence and metal-binding properties. The Journal of Biological Chemistry. 260: 14464-70. PMID 3902832 |
0.371 |
|
| 1984 |
Winge DR. Normal physiology of copper metabolism Seminars in Liver Disease. 4: 239-251. PMID 6385271 DOI: 10.1055/S-2008-1041774 |
0.336 |
|
| 1984 |
Geller BL, Winge DR. Subcellular distribution of superoxide dismutases in rat liver Methods in Enzymology. 105-114. PMID 6328174 DOI: 10.1016/S0076-6879(84)05014-X |
0.385 |
|
| 1983 |
Geller BL, Winge DR. A method for distinguishing Cu,Zn- and Mn-containing superoxide dismutases Analytical Biochemistry. 128: 86-92. PMID 6846803 DOI: 10.1016/0003-2697(83)90348-2 |
0.458 |
|
| 1983 |
Winge DR, Nielson KB. Formation of the metal-thiolate clusters of rat liver metallothionein Environmental Health Perspectives. 129-133. PMID 6734551 DOI: 10.1289/Ehp.8454129 |
0.302 |
|
| 1983 |
Winge DR, Garvey JS. Antigenicity of metallothionein Proceedings of the National Academy of Sciences of the United States of America. 80: 2472-2476. PMID 6189123 DOI: 10.1073/Pnas.80.9.2472 |
0.31 |
|
| 1982 |
Winge DR, Miklossy KA. Differences in the polymorphic forms of metallothionein Archives of Biochemistry and Biophysics. 214: 80-88. PMID 6805441 DOI: 10.1016/0003-9861(82)90010-8 |
0.377 |
|
| 1982 |
Geller BL, Winge DR. Metal binding sites of rat liver Cu-thionein Archives of Biochemistry and Biophysics. 213: 109-117. PMID 6277248 DOI: 10.1016/0003-9861(82)90445-3 |
0.46 |
|
| 1981 |
Winge DR, Geller BL, Garvey J. Isolation of copper thionein from rat liver Archives of Biochemistry and Biophysics. 208: 160-166. PMID 7259175 DOI: 10.1016/0003-9861(81)90135-1 |
0.433 |
|
| 1978 |
Winge DR, Premakumar R, Rajagopalan KV. Studies on the zinc content of Cd-induced thionein Archives of Biochemistry and Biophysics. 188: 466-475. PMID 677909 DOI: 10.1016/S0003-9861(78)80031-9 |
0.321 |
|
| 1978 |
Winge DR, Southerland WM, Rajagopalan KV. Structural studies of the heme domain of sulfite oxidase: CNBr fragments Biochemistry. 17: 1846-1853. PMID 656365 DOI: 10.1021/Bi00603A007 |
0.333 |
|
| 1975 |
Premakumar R, Winge DR, Wiley RD, Rajagopalan KV. Copper-induced synthesis of copper-chelatin in rat liver. Archives of Biochemistry and Biophysics. 170: 267-77. PMID 1164032 DOI: 10.1016/0003-9861(75)90117-4 |
0.422 |
|
| 1975 |
Premakumar R, Winge DR, Wiley RD, Rajagopalan KV. Copper-chelatin: isolation from various eucaryotic sources. Archives of Biochemistry and Biophysics. 170: 278-88. PMID 169747 DOI: 10.1016/0003-9861(75)90118-6 |
0.439 |
|
| 1975 |
Winge DR, Premakumar R, Wiley RD, Rajagopalan KV. Copper-chelatin: Purification and properties of a copper-binding protein from rat liver Archives of Biochemistry and Biophysics. 170: 253-266. PMID 169746 DOI: 10.1016/0003-9861(75)90116-2 |
0.465 |
|
| 1973 |
Winge DR, Rajagopalan KV. Purification and some properties of Cd-binding protein from rat liver. Archives of Biochemistry and Biophysics. 153: 755-62. PMID 4662108 DOI: 10.1016/0003-9861(72)90395-5 |
0.308 |
|
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