| Year |
Citation |
Score |
| 2024 |
Yang F, Smith MJ, Siow RCM, Aarsland D, Maret W, Mann GE. Interactions between zinc and NRF2 in vascular redox signalling. Biochemical Society Transactions. 52: 269-278. PMID 38372426 DOI: 10.1042/BST20230490 |
0.303 |
|
| 2023 |
Maret W. Chemistry meets biology in the coordination dynamics of metalloproteins. Journal of Inorganic Biochemistry. 251: 112431. PMID 38016325 DOI: 10.1016/j.jinorgbio.2023.112431 |
0.348 |
|
| 2021 |
Krężel A, Maret W. The Bioinorganic Chemistry of Mammalian Metallothioneins. Chemical Reviews. 121: 14594-14648. PMID 34652893 DOI: 10.1021/acs.chemrev.1c00371 |
0.369 |
|
| 2021 |
Catapano MC, Parsons DS, Kotuniak R, Mladěnka P, Bal W, Maret W. Probing the Structure and Function of the Cytosolic Domain of the Human Zinc Transporter ZnT8 with Nickel(II) Ions. International Journal of Molecular Sciences. 22. PMID 33799326 DOI: 10.3390/ijms22062940 |
0.366 |
|
| 2020 |
Frangos T, Maret W. Zinc and Cadmium in the Aetiology and Pathogenesis of Osteoarthritis and Rheumatoid Arthritis. Nutrients. 13. PMID 33375344 DOI: 10.3390/nu13010053 |
0.331 |
|
| 2020 |
Nimmanon T, Ziliotto S, Ogle O, Burt A, Gee JMW, Andrews GK, Kille P, Hogstrand C, Maret W, Taylor KM. The ZIP6/ZIP10 heteromer is essential for the zinc-mediated trigger of mitosis. Cellular and Molecular Life Sciences : Cmls. PMID 32797246 DOI: 10.1007/S00018-020-03616-6 |
0.376 |
|
| 2020 |
Muraina IA, Maret W, Bury NR, Hogstrand C. Hatching gland development and hatching in zebrafish embryos: A role for zinc and its transporters Zip10 and Znt1a. Biochemical and Biophysical Research Communications. PMID 32517868 DOI: 10.1016/J.Bbrc.2020.05.131 |
0.374 |
|
| 2019 |
Lawson R, Maret W, Hogstrand C. ZnT8 Haploinsufficiency Impacts MIN6 Cell Zinc Content and β-Cell Phenotype via ZIP-ZnT8 Coregulation. International Journal of Molecular Sciences. 20. PMID 31690008 DOI: 10.3390/Ijms20215485 |
0.31 |
|
| 2019 |
Moore RET, Rehkämper M, Maret W, Larner F. Assessment of coupled Zn concentration and natural stable isotope analyses of urine as a novel probe of Zn status. Metallomics : Integrated Biometal Science. PMID 31411226 DOI: 10.1039/C9Mt00160C |
0.353 |
|
| 2019 |
Maret W. Chromium Supplementation in Human Health, Metabolic Syndrome, and Diabetes. Metal Ions in Life Sciences. 19. PMID 30855110 DOI: 10.1515/9783110527872-015 |
0.301 |
|
| 2019 |
Maret W. The redox biology of redox-inert zinc ions. Free Radical Biology and Medicine. 134: 311-326. PMID 30625394 DOI: 10.1016/J.Freeradbiomed.2019.01.006 |
0.52 |
|
| 2018 |
Lawson R, Maret W, Hogstrand C. Prolonged stimulation of insulin release from MIN6 cells causes zinc depletion and loss of β-cell markers. Journal of Trace Elements in Medicine and Biology : Organ of the Society For Minerals and Trace Elements (Gms). 49: 51-59. PMID 29895372 DOI: 10.1016/J.Jtemb.2018.04.020 |
0.311 |
|
| 2018 |
Maret W. Metallomics: the science of biometals and biometalloids Advances in Experimental Medicine and Biology. 1055: 1-20. PMID 29884959 DOI: 10.1007/978-3-319-90143-5_1 |
0.356 |
|
| 2018 |
Bellomo E, Abro A, Hogstrand C, Maret W, Domene C. Role of zinc and magnesium ions in the modulation of phosphoryl transfer in protein tyrosine phosphatase 1B. Journal of the American Chemical Society. PMID 29512390 DOI: 10.1021/Jacs.8B01534 |
0.449 |
|
| 2018 |
Parsons DS, Hogstrand C, Maret W. The C-terminal cytosolic domain of the human zinc transporter ZnT8 and its diabetes risk variant. The Febs Journal. PMID 29430817 DOI: 10.1111/Febs.14402 |
0.346 |
|
| 2017 |
Maret W. Zinc in Cellular Regulation: The Nature and Significance of "Zinc Signals" International Journal of Molecular Sciences. 18: 2285. PMID 29088067 DOI: 10.3390/Ijms18112285 |
0.443 |
|
| 2017 |
Carvalho S, Molina-López J, Parsons D, Corpe C, Maret W, Hogstrand C. Differential cytolocation and functional assays of the two major human SLC30A8 (ZnT8) isoforms. Journal of Trace Elements in Medicine and Biology : Organ of the Society For Minerals and Trace Elements (Gms). 44: 116-124. PMID 28965566 DOI: 10.1016/J.Jtemb.2017.06.001 |
0.307 |
|
| 2017 |
Krężel A, Maret W. The functions of metamorphic metallothioneins in zinc and copper metabolism International Journal of Molecular Sciences. 18: 1237. PMID 28598392 DOI: 10.3390/Ijms18061237 |
0.466 |
|
| 2017 |
Singh KB, Maret W. The interactions of metal cations and oxyanions with protein tyrosine phosphatase 1B. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. PMID 28540523 DOI: 10.1007/S10534-017-0019-9 |
0.443 |
|
| 2017 |
Maret W. Zinc in Pancreatic Islet Biology, Insulin Sensitivity, and Diabetes. Journal of Food Science and Nutrition. 22: 1-8. PMID 28401081 DOI: 10.3746/Pnf.2017.22.1.1 |
0.383 |
|
| 2016 |
Bellomo E, Birla Singh K, Massarotti A, Hogstrand C, Maret W. The metal face of protein tyrosine phosphatase 1B. Coordination Chemistry Reviews. 327: 70-83. PMID 27890939 DOI: 10.1016/J.Ccr.2016.07.002 |
0.472 |
|
| 2016 |
Krężel A, Maret W. The biological inorganic chemistry of zinc ions. Archives of Biochemistry and Biophysics. PMID 27117234 DOI: 10.1016/J.Abb.2016.04.010 |
0.491 |
|
| 2015 |
Kasana S, Din J, Maret W. Genetic causes and gene–nutrient interactions in mammalian zinc deficiencies: acrodermatitis enteropathica and transient neonatal zinc deficiency as examples. Journal of Trace Elements in Medicine and Biology : Organ of the Society For Minerals and Trace Elements (Gms). 29: 47-62. PMID 25468189 DOI: 10.1016/J.Jtemb.2014.10.003 |
0.333 |
|
| 2015 |
Maret W. Analyzing free zinc(II) ion concentrations in cell biology with fluorescent chelating molecules. Metallomics : Integrated Biometal Science. 7: 202-11. PMID 25362967 DOI: 10.1039/C4Mt00230J |
0.468 |
|
| 2014 |
Bellomo E, Hogstrand C, Maret W. Redox and zinc signalling pathways converging on protein tyrosine phosphatases. Free Radical Biology & Medicine. 75: S9. PMID 26461422 DOI: 10.1016/J.Freeradbiomed.2014.10.851 |
0.471 |
|
| 2014 |
Maret W. Zinc in the biosciences. Metallomics : Integrated Biometal Science. 6: 1174. PMID 24942052 DOI: 10.1039/C4Mt90021A |
0.424 |
|
| 2014 |
Bellomo E, Massarotti A, Hogstrand C, Maret W. Zinc ions modulate protein tyrosine phosphatase 1B activity. Metallomics : Integrated Biometal Science. 6: 1229-39. PMID 24793162 DOI: 10.1039/C4Mt00086B |
0.46 |
|
| 2013 |
Maret W. Zinc and human disease. Metal Ions in Life Sciences. 13: 389-414. PMID 24470098 DOI: 10.1007/978-94-007-7500-8_12 |
0.485 |
|
| 2013 |
Maret W. Zinc and the zinc proteome. Metal Ions in Life Sciences. 12: 479-501. PMID 23595681 DOI: 10.1007/978-94-007-5561-1_14 |
0.472 |
|
| 2013 |
Maret W. Inhibitory zinc sites in enzymes. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. 26: 197-204. PMID 23456096 DOI: 10.1007/S10534-013-9613-7 |
0.478 |
|
| 2013 |
Maret W, Moulis JM. The bioinorganic chemistry of cadmium in the context of its toxicity. Metal Ions in Life Sciences. 11: 1-29. PMID 23430768 DOI: 10.1007/978-94-007-5179-8_1 |
0.34 |
|
| 2013 |
Maret W. Zinc biochemistry: from a single zinc enzyme to a key element of life. Advances in Nutrition (Bethesda, Md.). 4: 82-91. PMID 23319127 DOI: 10.3945/An.112.003038 |
0.51 |
|
| 2012 |
Wilson M, Hogstrand C, Maret W. Picomolar concentrations of free zinc(II) ions regulate receptor protein-tyrosine phosphatase β activity. The Journal of Biological Chemistry. 287: 9322-6. PMID 22275360 DOI: 10.1074/Jbc.C111.320796 |
0.452 |
|
| 2012 |
Maret W. New perspectives of zinc coordination environments in proteins. Journal of Inorganic Biochemistry. 111: 110-6. PMID 22196021 DOI: 10.1016/J.Jinorgbio.2011.11.018 |
0.494 |
|
| 2011 |
Maret W. Redox biochemistry of mammalian metallothioneins. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 16: 1079-86. PMID 21647775 DOI: 10.1007/S00775-011-0800-0 |
0.503 |
|
| 2011 |
Maret W. Metals on the move: zinc ions in cellular regulation and in the coordination dynamics of zinc proteins. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. 24: 411-8. PMID 21221719 DOI: 10.1007/S10534-010-9406-1 |
0.481 |
|
| 2010 |
Colvin RA, Holmes WR, Fontaine CP, Maret W. Cytosolic zinc buffering and muffling: Their role in intracellular zinc homeostasis Metallomics. 2: 306-317. PMID 21069178 DOI: 10.1039/B926662C |
0.463 |
|
| 2010 |
Maret W. Metalloproteomics, metalloproteomes, and the annotation of metalloproteins. Metallomics : Integrated Biometal Science. 2: 117-25. PMID 21069142 DOI: 10.1039/B915804A |
0.417 |
|
| 2010 |
Bozym RA, Chimienti F, Giblin LJ, Gross GW, Korichneva I, Li Y, Libert S, Maret W, Parviz M, Frederickson CJ, Thompson RB. Free zinc ions outside a narrow concentration range are toxic to a variety of cells in vitro. Experimental Biology and Medicine (Maywood, N.J.). 235: 741-50. PMID 20511678 DOI: 10.1258/Ebm.2010.009258 |
0.436 |
|
| 2010 |
Li Y, Hawkins BE, DeWitt DS, Prough DS, Maret W. The relationship between transient zinc ion fluctuations and redox signaling in the pathways of secondary cellular injury: relevance to traumatic brain injury. Brain Research. 1330: 131-41. PMID 20303343 DOI: 10.1016/J.Brainres.2010.03.034 |
0.367 |
|
| 2009 |
Maret W, Li Y. Coordination dynamics of zinc in proteins. Chemical Reviews. 109: 4682-707. PMID 19728700 DOI: 10.1021/Cr800556U |
0.349 |
|
| 2009 |
Maret W. Fluorescent probes for the structure and function of metallothionein. Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences. 877: 3378-83. PMID 19589737 DOI: 10.1016/J.Jchromb.2009.06.014 |
0.347 |
|
| 2009 |
Li Y, Maret W. Transient fluctuations of intracellular zinc ions in cell proliferation. Experimental Cell Research. 315: 2463-70. PMID 19467229 DOI: 10.1016/J.Yexcr.2009.05.016 |
0.377 |
|
| 2009 |
Maret W. Molecular aspects of human cellular zinc homeostasis: redox control of zinc potentials and zinc signals. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. 22: 149-57. PMID 19130267 DOI: 10.1007/S10534-008-9186-Z |
0.504 |
|
| 2008 |
Haase H, Maret W. Partial oxidation and oxidative polymerization of metallothionein. Electrophoresis. 29: 4169-76. PMID 18844317 DOI: 10.1002/Elps.200700922 |
0.363 |
|
| 2008 |
Maret W. A role for metallothionein in the pathogenesis of diabetes and its cardiovascular complications. Molecular Genetics and Metabolism. 94: 1-3. PMID 18321746 DOI: 10.1016/J.Ymgme.2008.01.010 |
0.383 |
|
| 2008 |
Maret W. Metallothionein redox biology in the cytoprotective and cytotoxic functions of zinc. Experimental Gerontology. 43: 363-9. PMID 18171607 DOI: 10.1016/J.Exger.2007.11.005 |
0.508 |
|
| 2008 |
Krezel A, Maret W. Thionein/metallothionein control Zn(II) availability and the activity of enzymes. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 13: 401-9. PMID 18074158 DOI: 10.1007/S00775-007-0330-Y |
0.388 |
|
| 2008 |
Maret W, Sandstead HH. Possible roles of zinc nutriture in the fetal origins of disease. Experimental Gerontology. 43: 378-81. PMID 18031964 DOI: 10.1016/J.Exger.2007.10.005 |
0.344 |
|
| 2008 |
Maret W. Zinc proteomics and the annotation of the human zinc proteome Pure and Applied Chemistry. 80: 2679-2687. DOI: 10.1351/Pac200880122679 |
0.469 |
|
| 2008 |
Li Y, Maret W. Human metallothionein metallomics Journal of Analytical Atomic Spectrometry. 23: 1055-1062. DOI: 10.1039/B802220H |
0.46 |
|
| 2007 |
Krezel A, Maret W. Dual nanomolar and picomolar Zn(II) binding properties of metallothionein. Journal of the American Chemical Society. 129: 10911-21. PMID 17696343 DOI: 10.1021/Ja071979S |
0.39 |
|
| 2007 |
Maret W, Krezel A. Cellular zinc and redox buffering capacity of metallothionein/thionein in health and disease. Molecular Medicine (Cambridge, Mass.). 13: 371-5. PMID 17622324 DOI: 10.2119/2007-00036.Maret |
0.499 |
|
| 2007 |
Krezel A, Hao Q, Maret W. The zinc/thiolate redox biochemistry of metallothionein and the control of zinc ion fluctuations in cell signaling. Archives of Biochemistry and Biophysics. 463: 188-200. PMID 17391643 DOI: 10.1016/J.Abb.2007.02.017 |
0.436 |
|
| 2007 |
Krezel A, Maret W. Different redox states of metallothionein/thionein in biological tissue. The Biochemical Journal. 402: 551-8. PMID 17134375 DOI: 10.1042/Bj20061044 |
0.481 |
|
| 2007 |
Hao Q, Hong SH, Maret W. Lipid raft-dependent endocytosis of metallothionein in HepG2 cells. Journal of Cellular Physiology. 210: 428-35. PMID 17111383 DOI: 10.1002/Jcp.20874 |
0.32 |
|
| 2006 |
Maret W. Zinc coordination environments in proteins as redox sensors and signal transducers. Antioxidants & Redox Signaling. 8: 1419-41. PMID 16987000 DOI: 10.1089/Ars.2006.8.1419 |
0.456 |
|
| 2006 |
Hao Q, Maret W. Aldehydes release zinc from proteins. A pathway from oxidative stress/lipid peroxidation to cellular functions of zinc. The Febs Journal. 273: 4300-10. PMID 16930132 DOI: 10.1111/J.1742-4658.2006.05428.X |
0.428 |
|
| 2006 |
Krezel A, Maret W. Zinc-buffering capacity of a eukaryotic cell at physiological pZn. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 1049-62. PMID 16924557 DOI: 10.1007/S00775-006-0150-5 |
0.434 |
|
| 2006 |
Maret W, Sandstead HH. Zinc requirements and the risks and benefits of zinc supplementation. Journal of Trace Elements in Medicine and Biology : Organ of the Society For Minerals and Trace Elements (Gms). 20: 3-18. PMID 16632171 DOI: 10.1016/J.Jtemb.2006.01.006 |
0.379 |
|
| 2005 |
Hao Q, Maret W. Imbalance between pro-oxidant and pro-antioxidant functions of zinc in disease. Journal of Alzheimer's Disease : Jad. 8: 161-70; discussion 2. PMID 16308485 DOI: 10.3233/Jad-2005-8209 |
0.468 |
|
| 2005 |
Haase H, Maret W. Fluctuations of cellular, available zinc modulate insulin signaling via inhibition of protein tyrosine phosphatases. Journal of Trace Elements in Medicine and Biology : Organ of the Society For Minerals and Trace Elements (Gms). 19: 37-42. PMID 16240670 DOI: 10.1016/J.Jtemb.2005.02.004 |
0.407 |
|
| 2005 |
Maret W. Zinc coordination environments in proteins determine zinc functions. Journal of Trace Elements in Medicine and Biology : Organ of the Society For Minerals and Trace Elements (Gms). 19: 7-12. PMID 16240665 DOI: 10.1016/J.Jtemb.2005.02.003 |
0.498 |
|
| 2005 |
Haase H, Maret W. Protein tyrosine phosphatases as targets of the combined insulinomimetic effects of zinc and oxidants. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. 18: 333-8. PMID 16158225 DOI: 10.1007/S10534-005-3707-9 |
0.376 |
|
| 2005 |
Feng W, Cai J, Pierce WM, Franklin RB, Maret W, Benz FW, Kang YJ. Metallothionein transfers zinc to mitochondrial aconitase through a direct interaction in mouse hearts. Biochemical and Biophysical Research Communications. 332: 853-8. PMID 15913554 DOI: 10.1016/J.Bbrc.2005.04.170 |
0.394 |
|
| 2004 |
Haase H, Maret W. A differential assay for the reduced and oxidized states of metallothionein and thionein. Analytical Biochemistry. 333: 19-26. PMID 15351276 DOI: 10.1016/J.Ab.2004.04.039 |
0.447 |
|
| 2004 |
Maret W. Zinc and sulfur: a critical biological partnership. Biochemistry. 43: 3301-9. PMID 15035601 DOI: 10.1021/Bi036340P |
0.394 |
|
| 2004 |
Frederickson CJ, Maret W, Cuajungco MP. Zinc and excitotoxic brain injury: a new model. The Neuroscientist : a Review Journal Bringing Neurobiology, Neurology and Psychiatry. 10: 18-25. PMID 14987444 DOI: 10.1177/1073858403255840 |
0.326 |
|
| 2004 |
Maret W. Exploring the zinc proteome Journal of Analytical Atomic Spectrometry. 19: 15-19. DOI: 10.1039/B307540K |
0.446 |
|
| 2003 |
Haase H, Maret W. Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling. Experimental Cell Research. 291: 289-98. PMID 14644152 DOI: 10.1016/S0014-4827(03)00406-3 |
0.36 |
|
| 2003 |
Maret W. Cellular zinc and redox states converge in the metallothionein/thionein pair. The Journal of Nutrition. 133: 1460S-2S. PMID 12730443 DOI: 10.1093/Jn/133.5.1460S |
0.484 |
|
| 2003 |
Hong SH, Maret W. A fluorescence resonance energy transfer sensor for the beta-domain of metallothionein. Proceedings of the National Academy of Sciences of the United States of America. 100: 2255-60. PMID 12618543 DOI: 10.1073/Pnas.0438005100 |
0.37 |
|
| 2002 |
Chen Y, Irie Y, Keung WM, Maret W. S-nitrosothiols react preferentially with zinc thiolate clusters of metallothionein III through transnitrosation. Biochemistry. 41: 8360-7. PMID 12081484 DOI: 10.1021/bi020030 |
0.375 |
|
| 2002 |
Maret W. Optical methods for measuring zinc binding and release, zinc coordination environments in zinc finger proteins, and redox sensitivity and activity of zinc-bound thiols. Methods in Enzymology. 348: 230-7. PMID 11885276 DOI: 10.1016/S0076-6879(02)48641-7 |
0.516 |
|
| 2002 |
Maret W, Heffron G, Hill HAO, Djuricic D, Jiang LJ, Vallee BL. The ATP/metallothionein interaction: NMR and STM Biochemistry. 41: 1689-1694. PMID 11814364 DOI: 10.1021/Bi0116083 |
0.318 |
|
| 2001 |
Maret W. Crosstalk of the group IIa and IIb metals calcium and zinc in cellular signaling. Proceedings of the National Academy of Sciences of the United States of America. 98: 12325-12327. PMID 11675482 DOI: 10.1073/Pnas.231481398 |
0.431 |
|
| 2001 |
Chen Y, Maret W. Catalytic oxidation of zinc/sulfur coordination sites in proteins by selenium compounds. Antioxidants & Redox Signaling. 3: 651-656. PMID 11554451 DOI: 10.1089/15230860152542998 |
0.431 |
|
| 2001 |
Chen Y, Maret W. Catalytic selenols couple the redox cycles of metallothionein and glutathione. Febs Journal. 268: 3346-3353. PMID 11389738 DOI: 10.1046/J.1432-1327.2001.02250.X |
0.405 |
|
| 2001 |
Maret W, Yetman CA, Jiang L. Enzyme regulation by reversible zinc inhibition: glycerol phosphate dehydrogenase as an example. Chemico-Biological Interactions. 130: 891-901. PMID 11306104 DOI: 10.1016/S0009-2797(00)00243-X |
0.424 |
|
| 2001 |
Ye B, Maret W, Vallee BL. Zinc metallothionein imported into liver mitochondria modulates respiration Proceedings of the National Academy of Sciences of the United States of America. 98: 2317-2322. PMID 11226237 DOI: 10.1073/Pnas.041619198 |
0.341 |
|
| 2001 |
Hong S, Toyama M, Maret W, Murooka Y. High yield expression and single step purification of human thionein/metallothionein. Protein Expression and Purification. 21: 243-250. PMID 11162412 DOI: 10.1006/Prep.2000.1372 |
0.365 |
|
| 2001 |
Lee S, Maret W. Redox Control of Zinc Finger Proteins: Mechanisms and Role in Gene Regulation Antioxidants & Redox Signaling. 3: 531-534. DOI: 10.1089/15230860152542907 |
0.487 |
|
| 2001 |
Maret W. Zinc biochemistry, physiology, and homeostasis – recent insights and current trends Biometals. 14: 187-190. DOI: 10.1023/A:1012945110820 |
0.308 |
|
| 2000 |
Maret W. The function of zinc metallothionein: a link between cellular zinc and redox state. Journal of Nutrition. 130. PMID 10801959 DOI: 10.1093/Jn/130.5.1455S |
0.442 |
|
| 2000 |
Jiang LJ, Vašák M, Vallee BL, Maret W. Zinc transfer potentials of the α- and β-clusters of metallothionein are affected by domain interactions in the whole molecule Proceedings of the National Academy of Sciences of the United States of America. 97: 2503-2508. PMID 10716985 DOI: 10.1073/Pnas.97.6.2503 |
0.303 |
|
| 1999 |
Maret W, Jacob C, Vallee BL, Fischer EH. Inhibitory sites in enzymes: Zinc removal and reactivation by thionein Proceedings of the National Academy of Sciences of the United States of America. 96: 1936-1940. PMID 10051573 DOI: 10.1073/Pnas.96.5.1936 |
0.38 |
|
| 1999 |
Jacob C, Maret W, Vallee BL. Selenium redox biochemistry of zinc-sulfur coordination sites in proteins and enzymes Proceedings of the National Academy of Sciences of the United States of America. 96: 1910-1914. PMID 10051568 DOI: 10.1073/Pnas.96.5.1910 |
0.425 |
|
| 1998 |
Jacob C, Maret W, Vallee BL. Ebselen, a selenium-containing redox drug, releases zinc from metallothionein Biochemical and Biophysical Research Communications. 248: 569-573. PMID 9703967 DOI: 10.1006/Bbrc.1998.9026 |
0.391 |
|
| 1998 |
Jiang LJ, Maret W, Vallee BL. The ATP-metallothionein complex Proceedings of the National Academy of Sciences of the United States of America. 95: 9146-9149. PMID 9689048 DOI: 10.1073/Pnas.95.16.9146 |
0.403 |
|
| 1998 |
Jacob C, Maret W, Vallee BL. Control of zinc transfer between thionein, metallothionein, and zinc proteins Proceedings of the National Academy of Sciences of the United States of America. 95: 3489-3494. PMID 9520393 DOI: 10.1073/Pnas.95.7.3489 |
0.419 |
|
| 1998 |
Jiang LJ, Maret W, Vallee BL. The glutathione redox couple modulates zinc transfer from metallothionein to zinc-depleted sorbitol dehydrogenase Proceedings of the National Academy of Sciences of the United States of America. 95: 3483-3488. PMID 9520392 DOI: 10.1073/Pnas.95.7.3483 |
0.4 |
|
| 1998 |
Maret W, Vallee BL. Thiolate ligands in metallothionein confer redox activity on zinc clusters Proceedings of the National Academy of Sciences of the United States of America. 95: 3478-3482. PMID 9520391 DOI: 10.1073/Pnas.95.7.3478 |
0.426 |
|
| 1997 |
Maret W, Larsen KS, Vallee BL. Coordination dynamics of biological zinc "clusters" in metallothioneins and in the DNA-binding domain of the transcription factor Ga14 Proceedings of the National Academy of Sciences of the United States of America. 94: 2233-2237. PMID 9122177 DOI: 10.1073/Pnas.94.6.2233 |
0.407 |
|
| 1995 |
Maret W. Metallothionein/disulfide interactions, oxidative stress, and the mobilization of cellular zinc Neurochemistry International. 27: 111-117. PMID 7655343 DOI: 10.1016/0197-0186(94)00173-R |
0.44 |
|
| 1994 |
Maret W. Oxidative metal release from metallothionein via zinc-thiol/disulfide interchange Proceedings of the National Academy of Sciences of the United States of America. 91: 237-241. PMID 8278372 DOI: 10.1073/Pnas.91.1.237 |
0.419 |
|
| 1993 |
Maret W. Detecting metal-metal interactions and measuring distances between metal centers in metalloproteins Methods in Enzymology. 226: 594-618. PMID 8277885 DOI: 10.1016/0076-6879(93)26028-8 |
0.375 |
|
| 1989 |
Karlsson C, Maret W, Auld DS, Hoog JO, Jornvall H. Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme European Journal of Biochemistry. 186: 543-550. PMID 2691249 DOI: 10.1111/J.1432-1033.1989.Tb15240.X |
0.31 |
|
| 1988 |
Maret W, Zeppezauer M. [9] Preparation of metal-hybrid enzymes Methods in Enzymology. 158: 79-94. PMID 3287097 DOI: 10.1016/0076-6879(88)58049-7 |
0.399 |
|
| 1986 |
Maret W, Zeppezauer M. Influence of anions and pH on the conformational change of horse liver alcohol dehydrogenase induced by binding of oxidized nicotinamide adenine dinucleotide: binding of chloride to the catalytic metal ion. Biochemistry. 25: 1584-1588. PMID 3011067 DOI: 10.1021/Bi00355A020 |
0.371 |
|
| 1986 |
Kováň J, Matyska L, Zeppezauer M, Maret W. Binding of ligands to horse liver alcohol dehydrogenase lacking zinc ions at the active sites. Febs Journal. 155: 391-396. PMID 2937633 DOI: 10.1111/J.1432-1033.1986.Tb09503.X |
0.388 |
|
| 1986 |
Maret W, Shiemke AK, Wheeler WD, Loehr TM, Sanders-Loehr J. Resonance Raman spectroscopy of blue copper proteins: ligand and coenzyme effects in copper(II)-substituted liver alcohol dehydrogenase Journal of the American Chemical Society. 108: 6351-6359. DOI: 10.1021/Ja00280A036 |
0.332 |
|
| 1983 |
Maret W, Zeppezauer M, Sanders-Loehr J, Loehr TM. Resonance Raman spectra of copper(II)-substituted liver alcohol dehydrogenase: a type 1 copper analogue. Biochemistry. 22: 3202-6. PMID 6349682 DOI: 10.1021/Bi00282A025 |
0.343 |
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| 1981 |
Andersson I, Maret W, Zeppezauer M, Brown RD, Koenig SH. Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 2. Binding of manganese(II) and competition with zinc(II) and cadmium(II) ions. Biochemistry. 20: 3433-8. PMID 7020752 DOI: 10.1021/Bi00515A020 |
0.374 |
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| 1981 |
Andersson I, Maret W, Zeppezauer M, Brown RD, Koenig SH. Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 1. Copper(II) and cobalt(II) ions. Biochemistry. 20: 3424-32. PMID 7020751 DOI: 10.1021/Bi00515A019 |
0.379 |
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