Year |
Citation |
Score |
2023 |
Kabin E, Dong Y, Roy S, Smirnova J, Smith JW, Ralle M, Summers K, Yang H, Dev S, Wang Y, Devenney B, Cole RN, Palumaa P, Lutsenko S. α-lipoic acid ameliorates consequences of copper overload by up-regulating selenoproteins and decreasing redox misbalance. Proceedings of the National Academy of Sciences of the United States of America. 120: e2305961120. PMID 37751556 DOI: 10.1073/pnas.2305961120 |
0.404 |
|
2023 |
Washington-Hughes CL, Roy S, Seneviratne HK, Karuppagounder SS, Morel Y, Jones JW, Zak A, Xiao T, Boronina TN, Cole RN, Bumpus NN, Chang CJ, Dawson TM, Lutsenko S. Atp7b-dependent choroid plexus dysfunction Causes transient copper deficit and metabolic changes in the developing mouse brain. Plos Genetics. 19: e1010558. PMID 36626371 DOI: 10.1371/journal.pgen.1010558 |
0.411 |
|
2022 |
McCann CJ, Hasan NM, Padilla-Benavides T, Roy S, Lutsenko S. Heterogeneous nuclear ribonucleoprotein hnRNPA2/B1 regulates the abundance of the copper-transporter ATP7A in an isoform-dependent manner. Frontiers in Molecular Biosciences. 9: 1067490. PMID 36545508 DOI: 10.3389/fmolb.2022.1067490 |
0.371 |
|
2022 |
Dev S, Muchenditsi A, Gottlieb A, Deme P, Murphy S, Gabrielson KL, Dong Y, Hughes R, Haughey NJ, Hamilton JP, Lutsenko S. Oxysterol misbalance critically contributes to Wilson disease pathogenesis. Science Advances. 8: eadc9022. PMID 36260680 DOI: 10.1126/sciadv.adc9022 |
0.371 |
|
2022 |
Dev S, Kruse RL, Hamilton JP, Lutsenko S. Wilson Disease: Update on Pathophysiology and Treatment. Frontiers in Cell and Developmental Biology. 10: 871877. PMID 35586338 DOI: 10.3389/fcell.2022.871877 |
0.389 |
|
2022 |
Tsvetkov P, Coy S, Petrova B, Dreishpoon M, Verma A, Abdusamad M, Rossen J, Joesch-Cohen L, Humeidi R, Spangler RD, Eaton JK, Frenkel E, Kocak M, Corsello SM, Lutsenko S, et al. Copper induces cell death by targeting lipoylated TCA cycle proteins. Science (New York, N.Y.). 375: 1254-1261. PMID 35298263 DOI: 10.1126/science.abf0529 |
0.352 |
|
2021 |
Ge EJ, Bush AI, Casini A, Cobine PA, Cross JR, DeNicola GM, Dou QP, Franz KJ, Gohil VM, Gupta S, Kaler SG, Lutsenko S, Mittal V, Petris MJ, Polishchuk R, et al. Connecting copper and cancer: from transition metal signalling to metalloplasia. Nature Reviews. Cancer. PMID 34764459 DOI: 10.1038/s41568-021-00417-2 |
0.353 |
|
2021 |
Lutsenko S. Dynamic and cell-specific transport networks for intracellular copper ions. Journal of Cell Science. 134. PMID 34734631 DOI: 10.1242/jcs.240523 |
0.411 |
|
2021 |
Muchenditsi A, Talbot CC, Gottlieb A, Yang H, Kang B, Boronina T, Cole R, Wang L, Dev S, Hamilton JP, Lutsenko S. Systemic deletion of Atp7b modifies the hepatocytes' response to copper overload in the mouse models of Wilson disease. Scientific Reports. 11: 5659. PMID 33707579 DOI: 10.1038/s41598-021-84894-3 |
0.373 |
|
2020 |
Uhlemann EE, Yu CH, Patry J, Dolgova N, Lutsenko S, Muyldermans S, Dmitriev OY. Nanobodies against the metal binding domains of ATP7B as tools to study copper transport in the cell. Metallomics : Integrated Biometal Science. PMID 33094790 DOI: 10.1039/d0mt00191k |
0.36 |
|
2020 |
Roy S, McCann CJ, Ralle M, Ray K, Ray J, Lutsenko S, Jayakanthan S. Analysis of Wilson disease mutations revealed that interactions between different ATP7B mutants modify their properties. Scientific Reports. 10: 13487. PMID 32778786 DOI: 10.1038/S41598-020-70366-7 |
0.446 |
|
2020 |
Lutsenko S. Sending copper where it is needed most. Science (New York, N.Y.). 368: 584-585. PMID 32381707 DOI: 10.1126/science.abb6662 |
0.396 |
|
2020 |
Culbertson EM, Khan AA, Muchenditsi A, Lutsenko S, Sullivan DJ, Petris MJ, Cormack BP, Culotta VC. Changes in mammalian copper homeostasis during microbial infection. Metallomics : Integrated Biometal Science. PMID 31976503 DOI: 10.1039/C9Mt00294D |
0.314 |
|
2019 |
Lutsenko S, Washington-Hughes C, Ralle M, Schmidt K. Copper and the brain noradrenergic system. Journal of Biological Inorganic Chemistry. 24: 1179-1188. PMID 31691104 DOI: 10.1007/S00775-019-01737-3 |
0.475 |
|
2019 |
Pierson H, Yang H, Lutsenko S. Copper Transport and Disease: What Can We Learn from Organoids? Annual Review of Nutrition. PMID 31150593 DOI: 10.1146/Annurev-Nutr-082018-124242 |
0.492 |
|
2019 |
McCann CJ, Jayakanthan S, Siotto M, Yang N, Osipova M, Squitti R, Lutsenko S. Single nucleotide polymorphisms in the human ATP7B gene modify the properties of the ATP7B protein. Metallomics : Integrated Biometal Science. PMID 31070637 DOI: 10.1039/C9Mt00057G |
0.386 |
|
2018 |
Schmidt K, Ralle M, Schaffer T, Jayakanthan S, Bari B, Muchenditsi A, Lutsenko S. ATP7A and ATP7B copper transporters have distinct functions in the regulation of neuronal DOPAMINE-β-HYDROXYLASE. The Journal of Biological Chemistry. PMID 30341172 DOI: 10.1074/jbc.RA118.004889 |
0.372 |
|
2018 |
Yang H, Ralle M, Wolfgang MJ, Dhawan N, Burkhead JL, Rodriguez S, Kaplan JH, Wong GW, Haughey N, Lutsenko S. Copper-dependent amino oxidase 3 governs selection of metabolic fuels in adipocytes. Plos Biology. 16: e2006519. PMID 30199530 DOI: 10.1371/Journal.Pbio.2006519 |
0.479 |
|
2018 |
Członkowska A, Litwin T, Dusek P, Ferenci P, Lutsenko S, Medici V, Rybakowski JK, Weiss KH, Schilsky ML. Wilson disease. Nature Reviews. Disease Primers. 4: 21. PMID 30190489 DOI: 10.1038/s41572-018-0018-3 |
0.354 |
|
2018 |
Reed E, Lutsenko S, Bandmann O. Animal models of Wilson disease. Journal of Neurochemistry. PMID 29473169 DOI: 10.1111/Jnc.14323 |
0.357 |
|
2017 |
Pierson H, Muchenditsi A, Kim BE, Ralle M, Zachos N, Huster D, Lutsenko S. The Function of ATPase Copper Transporter ATP7B in Intestine. Gastroenterology. PMID 28958857 DOI: 10.1053/j.gastro.2017.09.019 |
0.438 |
|
2017 |
Yu CH, Yang N, Bothe J, Tonelli M, Nokhrin S, Dolgova NV, Braiterman LT, Lutsenko S, Dmitriev OY. The metal chaperone Atox1 regulates the activity of the human copper transporter ATP7B by modulating domain dynamics. The Journal of Biological Chemistry. PMID 28900031 DOI: 10.1074/Jbc.M117.811752 |
0.448 |
|
2017 |
Jayakanthan S, Braiterman LT, Hasan NM, Unger VM, Lutsenko S. HUMAN COPPER TRANSPORTER ATP7B (WILSON DISEASE PROTEIN) FORMS STABLE DIMERS IN VITRO AND IN CELLS. The Journal of Biological Chemistry. PMID 28842499 DOI: 10.1074/Jbc.M117.807263 |
0.519 |
|
2017 |
Muchenditsi A, Yang H, Hamilton JP, Koganti L, Housseau F, Aronov L, Fan H, Pierson H, Bhattacharjee A, Murphy RC, Sears CL, Potter JJ, Wooton-Kee CR, Lutsenko S. TARGETED INACTIVATION OF COPPER-TRANSPORTER ATP7B IN HEPATOCYTES CAUSES LIVER STEATOSIS AND OBESITY IN MICE. American Journal of Physiology. Gastrointestinal and Liver Physiology. ajpgi.00312.2016. PMID 28428350 DOI: 10.1152/Ajpgi.00312.2016 |
0.485 |
|
2016 |
Lutsenko S. Copper trafficking to the secretory pathway. Metallomics : Integrated Biometal Science. 8: 840-52. PMID 27603756 DOI: 10.1039/c6mt00176a |
0.385 |
|
2016 |
Hatori Y, Lutsenko S. The Role of Copper Chaperone Atox1 in Coupling Redox Homeostasis to Intracellular Copper Distribution. Antioxidants (Basel, Switzerland). 5. PMID 27472369 DOI: 10.3390/antiox5030025 |
0.412 |
|
2016 |
Lee S, Barin G, Ackerman CM, Muchenditsi A, Xu J, Reimer JA, Lutsenko S, Long JR, Chang CJ. Copper Capture in a Thioether-Functionalized Porous Polymer Applied to the Detection of Wilson's Disease. Journal of the American Chemical Society. PMID 27285482 DOI: 10.1021/Jacs.6B02515 |
0.336 |
|
2016 |
Krishnamoorthy L, Cotruvo JA, Chan J, Kaluarachchi H, Muchenditsi A, Pendyala VS, Jia S, Aron AT, Ackerman CM, Wal MN, Guan T, Smaga LP, Farhi SL, New EJ, Lutsenko S, et al. Copper regulates cyclic-AMP-dependent lipolysis. Nature Chemical Biology. PMID 27272565 DOI: 10.1038/Nchembio.2098 |
0.495 |
|
2016 |
Kline CD, Gambill BF, Mayfield M, Lutsenko S, Blackburn NJ. pH-regulated metal-ligand switching in the HM loop of ATP7A: a new paradigm for metal transfer chemistry. Metallomics : Integrated Biometal Science. PMID 27242196 DOI: 10.1039/C6Mt00062B |
0.362 |
|
2016 |
Bhattacharjee A, Yang H, Duffy M, Robinson E, Conrad-Antoville A, Lu YW, Capps T, Braiterman LT, Wolfgang MJ, Murphy MP, Yi L, Kaler SG, Lutsenko S, Ralle M. Activity of Menkes Disease Protein ATP7A is Essential for Redox Balance in Mitochondria. The Journal of Biological Chemistry. PMID 27226607 DOI: 10.1074/Jbc.M116.727248 |
0.458 |
|
2016 |
Hatori Y, Yan Y, Schmidt K, Furukawa E, Hasan NM, Yang N, Liu CN, Sockanathan S, Lutsenko S. Neuronal differentiation is associated with a redox-regulated increase of copper flow to the secretory pathway. Nature Communications. 7: 10640. PMID 26879543 DOI: 10.1038/Ncomms10640 |
0.377 |
|
2016 |
Gupta A, Schell MJ, Bhattacharjee A, Lutsenko S, Hubbard AL. Myosin Vb mediates copper export in polarized hepatocytes. Journal of Cell Science. PMID 26823605 DOI: 10.1242/Jcs.175307 |
0.461 |
|
2016 |
Lutsenko S. Introduction to the Minireview Series on Modern Technologies for In-cell Biochemistry. The Journal of Biological Chemistry. 291: 3757-8. PMID 26677225 DOI: 10.1074/Jbc.R115.709444 |
0.313 |
|
2016 |
Chesi G, Hegde RN, Iacobacci S, Concilli M, Parashuraman S, Festa BP, Polishchuk EV, Di Tullio G, Carissimo A, Montefusco S, Canetti D, Monti M, Amoresano A, Pucci P, van de Sluis B, ... Lutsenko S, et al. Identification of p38 MAPK and JNK as new targets for correction of Wilson disease-causing ATP7B mutants. Hepatology (Baltimore, Md.). 63: 1842-59. PMID 26660341 DOI: 10.1002/Hep.28398 |
0.512 |
|
2015 |
Hamilton JP, Koganti L, Muchenditsi A, Pendyala VS, Huso D, Hankin J, Murphy RC, Huster D, Merle U, Mangels C, Yang N, Potter JJ, Mezey E, Lutsenko S. Activation of LXR/RXR pathway ameliorates liver disease in atp7b(-/-) (wilson disease) mice. Hepatology (Baltimore, Md.). PMID 26679751 DOI: 10.1002/Hep.28406 |
0.422 |
|
2015 |
Wooton-Kee CR, Jain AK, Wagner M, Grusak MA, Finegold MJ, Lutsenko S, Moore DD. Elevated copper impairs hepatic nuclear receptor function in Wilson's disease. The Journal of Clinical Investigation. PMID 26241054 DOI: 10.1172/Jci78991 |
0.458 |
|
2014 |
Huang Y, Nokhrin S, Hassanzadeh-Ghassabeh G, Yu CH, Yang H, Barry AN, Tonelli M, Markley JL, Muyldermans S, Dmitriev OY, Lutsenko S. Interactions between metal-binding domains modulate intracellular targeting of Cu(I)-ATPase ATP7B, as revealed by nanobody binding. The Journal of Biological Chemistry. 289: 32682-93. PMID 25253690 DOI: 10.1074/Jbc.M114.580845 |
0.393 |
|
2014 |
Graper ML, Huster D, Kaler SG, Lutsenko S, Schilsky ML, Thiele DJ. Introduction to Human Disorders of Copper Metabolism. Annals of the New York Academy of Sciences. 1314: v-vi. PMID 24820197 DOI: 10.1111/Nyas.12448 |
0.382 |
|
2014 |
Braiterman LT, Murthy A, Jayakanthan S, Nyasae L, Tzeng E, Gromadzka G, Woolf TB, Lutsenko S, Hubbard AL. Distinct phenotype of a Wilson disease mutation reveals a novel trafficking determinant in the copper transporter ATP7B. Proceedings of the National Academy of Sciences of the United States of America. 111: E1364-73. PMID 24706876 DOI: 10.1073/Pnas.1314161111 |
0.38 |
|
2014 |
Lutsenko S. Modifying factors and phenotypic diversity in Wilson's disease. Annals of the New York Academy of Sciences. 1315: 56-63. PMID 24702697 DOI: 10.1111/Nyas.12420 |
0.491 |
|
2014 |
Malinouski M, Hasan NM, Zhang Y, Seravalli J, Lin J, Avanesov A, Lutsenko S, Gladyshev VN. Genome-wide RNAi ionomics screen reveals new genes and regulation of human trace element metabolism. Nature Communications. 5: 3301. PMID 24522796 DOI: 10.1038/Ncomms4301 |
0.36 |
|
2014 |
Gupta A, Bhattacharjee A, Hasan N, Braiterman L, Lutsenko S, Hubbard AL. Genetic, metabolic and cellular factors influencing intracellular localization of the Wilson disease protein, ATP7B Molecular Cytogenetics. 7: P68. DOI: 10.1186/1755-8166-7-S1-P68 |
0.498 |
|
2014 |
Bhattacharjee A, Ralle M, Lutsenko S. Live-cell imaging of compartment-specific redox changes in menkes disease fibroblasts Molecular Cytogenetics. 7: 54. DOI: 10.1186/1755-8166-7-S1-P54 |
0.483 |
|
2013 |
Polishchuk R, Lutsenko S. Golgi in copper homeostasis: a view from the membrane trafficking field. Histochemistry and Cell Biology. 140: 285-95. PMID 23846821 DOI: 10.1007/S00418-013-1123-8 |
0.563 |
|
2013 |
Hatori Y, Lutsenko S. An expanding range of functions for the copper chaperone/antioxidant protein Atox1. Antioxidants & Redox Signaling. 19: 945-57. PMID 23249252 DOI: 10.1089/Ars.2012.5086 |
0.552 |
|
2012 |
Hasan NM, Lutsenko S. Regulation of copper transporters in human cells. Current Topics in Membranes. 69: 137-61. PMID 23046650 DOI: 10.1016/B978-0-12-394390-3.00006-9 |
0.515 |
|
2012 |
Gupta A, Lutsenko S. Evolution of copper transporting ATPases in eukaryotic organisms. Current Genomics. 13: 124-33. PMID 23024604 DOI: 10.2174/138920212799860661 |
0.55 |
|
2012 |
Hasan NM, Gupta A, Polishchuk E, Yu CH, Polishchuk R, Dmitriev OY, Lutsenko S. Molecular events initiating exit of a copper-transporting ATPase ATP7B from the trans-Golgi network. The Journal of Biological Chemistry. 287: 36041-50. PMID 22898812 DOI: 10.1074/Jbc.M112.370403 |
0.479 |
|
2012 |
Gray LW, Peng F, Molloy SA, Pendyala VS, Muchenditsi A, Muzik O, Lee J, Kaplan JH, Lutsenko S. Urinary copper elevation in a mouse model of Wilson's disease is a regulated process to specifically decrease the hepatic copper load. Plos One. 7: e38327. PMID 22802922 DOI: 10.1371/Journal.Pone.0038327 |
0.545 |
|
2012 |
Schushan M, Bhattacharjee A, Ben-Tal N, Lutsenko S. A structural model of the copper ATPase ATP7B to facilitate analysis of Wilson disease-causing mutations and studies of the transport mechanism. Metallomics : Integrated Biometal Science. 4: 669-78. PMID 22692182 DOI: 10.1039/C2Mt20025B |
0.45 |
|
2012 |
Hatori Y, Clasen S, Hasan NM, Barry AN, Lutsenko S. Functional partnership of the copper export machinery and glutathione balance in human cells. The Journal of Biological Chemistry. 287: 26678-87. PMID 22648419 DOI: 10.1074/Jbc.M112.381178 |
0.511 |
|
2012 |
Otoikhian A, Barry AN, Mayfield M, Nilges M, Huang Y, Lutsenko S, Blackburn NJ. Lumenal loop M672-P707 of the menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase Journal of the American Chemical Society. 134: 10458-10468. PMID 22577880 DOI: 10.1021/Ja301221S |
0.514 |
|
2012 |
Wilmarth PA, Short KK, Fiehn O, Lutsenko S, David LL, Burkhead JL. A systems approach implicates nuclear receptor targeting in the Atp7b -/- mouse model of Wilson's disease Metallomics. 4: 660-668. PMID 22565294 DOI: 10.1039/C2Mt20017A |
0.473 |
|
2012 |
Hirayama T, Van de Bittner GC, Gray LW, Lutsenko S, Chang CJ. Near-infrared fluorescent sensor for in vivo copper imaging in a murine Wilson disease model. Proceedings of the National Academy of Sciences of the United States of America. 109: 2228-33. PMID 22308360 DOI: 10.1073/Pnas.1113729109 |
0.497 |
|
2012 |
Huster D, Kühne A, Bhattacharjee A, Raines L, Jantsch V, Noe J, Schirrmeister W, Sommerer I, Sabri O, Berr F, Mössner J, Stieger B, Caca K, Lutsenko S. Diverse functional properties of Wilson disease ATP7B variants. Gastroenterology. 142: 947-956.e5. PMID 22240481 DOI: 10.1053/J.Gastro.2011.12.048 |
0.53 |
|
2012 |
Peng F, Lutsenko S, Sun X, Muzik O. Imaging copper metabolism imbalance in Atp7b (-/-) knockout mouse model of Wilson's disease with PET-CT and orally administered 64CuCl2. Molecular Imaging and Biology : Mib : the Official Publication of the Academy of Molecular Imaging. 14: 600-7. PMID 22170165 DOI: 10.1007/S11307-011-0532-0 |
0.351 |
|
2012 |
Peng F, Lutsenko S, Sun X, Muzik O. Positron emission tomography of copper metabolism in the Atp7b-/- knock-out mouse model of Wilson's disease. Molecular Imaging and Biology : Mib : the Official Publication of the Academy of Molecular Imaging. 14: 70-8. PMID 21327972 DOI: 10.1007/S11307-011-0476-4 |
0.392 |
|
2011 |
Barry AN, Otoikhian A, Bhatt S, Shinde U, Tsivkovskii R, Blackburn NJ, Lutsenko S. The lumenal loop Met672-Pro707 of copper-transporting ATPase ATP7A binds metals and facilitates copper release from the intramembrane sites. The Journal of Biological Chemistry. 286: 26585-94. PMID 21646353 DOI: 10.1074/Jbc.M111.229039 |
0.545 |
|
2011 |
Gupta A, Bhattacharjee A, Dmitriev OY, Nokhrin S, Braiterman L, Hubbard AL, Lutsenko S. Cellular copper levels determine the phenotype of the Arg875 variant of ATP7B/Wilson disease protein. Proceedings of the National Academy of Sciences of the United States of America. 108: 5390-5. PMID 21406592 DOI: 10.1073/Pnas.1014959108 |
0.557 |
|
2011 |
Dmitriev OY, Bhattacharjee A, Nokhrin S, Uhlemann EM, Lutsenko S. Difference in stability of the N-domain underlies distinct intracellular properties of the E1064A and H1069Q mutants of copper-transporting ATPase ATP7B. The Journal of Biological Chemistry. 286: 16355-62. PMID 21398519 DOI: 10.1074/Jbc.M110.198101 |
0.422 |
|
2011 |
Burkhead JL, Gray LW, Lutsenko S. Systems biology approach to Wilson's disease. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. 24: 455-66. PMID 21380607 DOI: 10.1007/S10534-011-9430-9 |
0.476 |
|
2011 |
Burkhead JL, Ralle M, Wilmarth P, David L, Lutsenko S. Elevated copper remodels hepatic RNA processing machinery in the mouse model of Wilson's disease. Journal of Molecular Biology. 406: 44-58. PMID 21146535 DOI: 10.1016/J.Jmb.2010.12.001 |
0.45 |
|
2010 |
Lutsenko S, Bhattacharjee A, Hubbard AL. Copper handling machinery of the brain. Metallomics : Integrated Biometal Science. 2: 596-608. PMID 21072351 DOI: 10.1039/C0Mt00006J |
0.499 |
|
2010 |
Ralle M, Huster D, Vogt S, Schirrmeister W, Burkhead JL, Capps TR, Gray L, Lai B, Maryon E, Lutsenko S. Wilson disease at a single cell level: intracellular copper trafficking activates compartment-specific responses in hepatocytes. The Journal of Biological Chemistry. 285: 30875-83. PMID 20647314 DOI: 10.1074/Jbc.M110.114447 |
0.54 |
|
2010 |
Lutsenko S. Human copper homeostasis: a network of interconnected pathways. Current Opinion in Chemical Biology. 14: 211-7. PMID 20117961 DOI: 10.1016/J.Cbpa.2010.01.003 |
0.527 |
|
2010 |
LeShane ES, Shinde U, Walker JM, Barry AN, Blackburn NJ, Ralle M, Lutsenko S. Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B. The Journal of Biological Chemistry. 285: 6327-36. PMID 20032459 DOI: 10.1074/Jbc.M109.074633 |
0.482 |
|
2010 |
Barry AN, Shinde U, Lutsenko S. Structural organization of human Cu-transporting ATPases: learning from building blocks. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 15: 47-59. PMID 19851794 DOI: 10.1007/S00775-009-0595-4 |
0.544 |
|
2009 |
Gupta A, Lutsenko S. Human copper transporters: mechanism, role in human diseases and therapeutic potential. Future Medicinal Chemistry. 1: 1125-42. PMID 20454597 DOI: 10.4155/Fmc.09.84 |
0.532 |
|
2009 |
Kaplan JH, Lutsenko S. Copper transport in mammalian cells: special care for a metal with special needs. The Journal of Biological Chemistry. 284: 25461-5. PMID 19602511 DOI: 10.1074/Jbc.R109.031286 |
0.513 |
|
2009 |
Wright LM, Huster D, Lutsenko S, Wrba F, Ferenci P, Fimmel CJ. Hepatocyte GP73 expression in Wilson disease Journal of Hepatology. 51: 557-564. PMID 19596473 DOI: 10.1016/J.Jhep.2009.05.029 |
0.367 |
|
2009 |
Barnes N, Bartee MY, Braiterman L, Gupta A, Ustiyan V, Zuzel V, Kaplan JH, Hubbard AL, Lutsenko S. Cell-specific trafficking suggests a new role for renal ATP7B in the intracellular copper storage. Traffic (Copenhagen, Denmark). 10: 767-79. PMID 19416479 DOI: 10.1111/J.1600-0854.2009.00901.X |
0.415 |
|
2009 |
Bartee MY, Ralle M, Lutsenko S. The loop connecting metal-binding domains 3 and 4 of ATP7B is a target of a kinase-mediated phosphorylation. Biochemistry. 48: 5573-81. PMID 19405516 DOI: 10.1021/Bi900325K |
0.4 |
|
2009 |
Dolgova NV, Olson D, Lutsenko S, Dmitriev OY. The soluble metal-binding domain of the copper transporter ATP7B binds and detoxifies cisplatin. The Biochemical Journal. 419: 51-6, 3 p following . PMID 19173677 DOI: 10.1042/Bj20081359 |
0.395 |
|
2009 |
Leonhardt K, Gebhardt R, Mössner J, Lutsenko S, Huster D. Functional interactions of Cu-ATPase ATP7B with cisplatin and the role of ATP7B in the resistance of cells to the drug. The Journal of Biological Chemistry. 284: 7793-802. PMID 19141620 DOI: 10.1074/Jbc.M805145200 |
0.47 |
|
2009 |
Braiterman L, Nyasae L, Guo Y, Bustos R, Lutsenko S, Hubbard A. Apical targeting and Golgi retention signals reside within a 9-amino acid sequence in the copper-ATPase, ATP7B. American Journal of Physiology. Gastrointestinal and Liver Physiology. 296: G433-44. PMID 19033537 DOI: 10.1152/Ajpgi.90489.2008 |
0.54 |
|
2009 |
Burkhead JL, Morgan CT, Shinde U, Haddock G, Lutsenko S. COMMD1 forms oligomeric complexes targeted to the endocytic membranes via specific interactions with phosphatidylinositol 4,5-bisphosphate. The Journal of Biological Chemistry. 284: 696-707. PMID 18940794 DOI: 10.1074/Jbc.M804766200 |
0.404 |
|
2008 |
Lutsenko S. Atp7b-/- mice as a model for studies of Wilson's disease. Biochemical Society Transactions. 36: 1233-8. PMID 19021531 DOI: 10.1042/Bst0361233 |
0.433 |
|
2008 |
Lutsenko S, Gupta A, Burkhead JL, Zuzel V. Cellular multitasking: the dual role of human Cu-ATPases in cofactor delivery and intracellular copper balance. Archives of Biochemistry and Biophysics. 476: 22-32. PMID 18534184 DOI: 10.1016/J.Abb.2008.05.005 |
0.557 |
|
2008 |
Lörinczi E, Tsivkovskii R, Haase W, Bamberg E, Lutsenko S, Friedrich T. Delivery of the Cu-transporting ATPase ATP7B to the plasma membrane in Xenopus oocytes. Biochimica Et Biophysica Acta. 1778: 896-906. PMID 18222167 DOI: 10.1016/J.Bbamem.2007.12.020 |
0.489 |
|
2008 |
Linz R, Barnes NL, Zimnicka AM, Kaplan JH, Eipper B, Lutsenko S. Intracellular targeting of copper-transporting ATPase ATP7A in a normal and Atp7b-/- kidney. American Journal of Physiology. Renal Physiology. 294: F53-61. PMID 17928409 DOI: 10.1152/Ajprenal.00314.2007 |
0.527 |
|
2007 |
Linz R, Lutsenko S. Copper-transporting ATPases ATP7A and ATP7B: cousins, not twins. Journal of Bioenergetics and Biomembranes. 39: 403-7. PMID 18000748 DOI: 10.1007/S10863-007-9101-2 |
0.529 |
|
2007 |
Huster D, Lutsenko S. Wilson disease: not just a copper disorder. Analysis of a Wilson disease model demonstrates the link between copper and lipid metabolism. Molecular Biosystems. 3: 816-24. PMID 18000558 DOI: 10.1039/B711118P |
0.53 |
|
2007 |
Lutsenko S, Barnes NL, Bartee MY, Dmitriev OY. Function and regulation of human copper-transporting ATPases. Physiological Reviews. 87: 1011-46. PMID 17615395 DOI: 10.1152/Physrev.00004.2006 |
0.56 |
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2007 |
Lutsenko S, LeShane ES, Shinde U. Biochemical basis of regulation of human copper-transporting ATPases. Archives of Biochemistry and Biophysics. 463: 134-48. PMID 17562324 DOI: 10.1016/J.Abb.2007.04.013 |
0.557 |
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2007 |
Bartee MY, Lutsenko S. Hepatic copper-transporting ATPase ATP7B: function and inactivation at the molecular and cellular level. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. 20: 627-37. PMID 17268820 DOI: 10.1007/S10534-006-9074-3 |
0.595 |
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2007 |
Huster D, Purnat TD, Burkhead JL, Ralle M, Fiehn O, Stuckert F, Olson NE, Teupser D, Lutsenko S. High copper selectively alters lipid metabolism and cell cycle machinery in the mouse model of Wilson disease. The Journal of Biological Chemistry. 282: 8343-55. PMID 17205981 DOI: 10.1074/Jbc.M607496200 |
0.492 |
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2006 |
Dmitriev OY, Tsivkovskii R, Abildgaard F, Lutsenko S. NMR assignment of the Wilson disease associated protein N-domain. Journal of Biomolecular Nmr. 36: 61. PMID 16868859 DOI: 10.1007/S10858-006-9046-5 |
0.316 |
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2006 |
Dmitriev O, Tsivkovskii R, Abildgaard F, Morgan CT, Markley JL, Lutsenko S. Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutations. Proceedings of the National Academy of Sciences of the United States of America. 103: 5302-7. PMID 16567646 DOI: 10.1073/Pnas.0507416103 |
0.446 |
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2006 |
Huster D, Finegold MJ, Morgan CT, Burkhead JL, Nixon R, Vanderwerf SM, Gilliam CT, Lutsenko S. Consequences of copper accumulation in the livers of the Atp7b-/- (Wilson disease gene) knockout mice. The American Journal of Pathology. 168: 423-34. PMID 16436657 DOI: 10.2353/Ajpath.2006.050312 |
0.49 |
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2005 |
Barnes N, Tsivkovskii R, Tsivkovskaia N, Lutsenko S. The copper-transporting ATPases, menkes and wilson disease proteins, have distinct roles in adult and developing cerebellum. The Journal of Biological Chemistry. 280: 9640-5. PMID 15634671 DOI: 10.1074/Jbc.M413840200 |
0.515 |
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2004 |
Morgan CT, Tsivkovskii R, Kosinsky YA, Efremov RG, Lutsenko S. The distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104F. The Journal of Biological Chemistry. 279: 36363-71. PMID 15205462 DOI: 10.1074/Jbc.M404553200 |
0.418 |
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2004 |
Efremov RG, Kosinsky YA, Nolde DE, Tsivkovskii R, Arseniev AS, Lutsenko S. Molecular modelling of the nucleotide-binding domain of Wilson's disease protein: location of the ATP-binding site, domain dynamics and potential effects of the major disease mutations. The Biochemical Journal. 382: 293-305. PMID 15147237 DOI: 10.1042/Bj20040326 |
0.408 |
|
2004 |
Ralle M, Lutsenko S, Blackburn NJ. Copper transfer to the N-terminal domain of the Wilson disease protein (ATP7B): X-ray absorption spectroscopy of reconstituted and chaperone-loaded metal binding domains and their interaction with exogenous ligands. Journal of Inorganic Biochemistry. 98: 765-74. PMID 15134922 DOI: 10.1016/J.Jinorgbio.2004.02.009 |
0.47 |
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2004 |
Walker JM, Huster D, Ralle M, Morgan CT, Blackburn NJ, Lutsenko S. The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1. The Journal of Biological Chemistry. 279: 15376-84. PMID 14754885 DOI: 10.1074/Jbc.M400053200 |
0.53 |
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2003 |
Huster D, Lutsenko S. The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein. The Journal of Biological Chemistry. 278: 32212-8. PMID 12794172 DOI: 10.1074/Jbc.M305408200 |
0.555 |
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2003 |
Lutsenko S, Tsivkovskii R, Walker JM. Functional properties of the human copper-transporting ATPase ATP7B (the Wilson's disease protein) and regulation by metallochaperone Atox1. Annals of the New York Academy of Sciences. 986: 204-11. PMID 12763797 DOI: 10.1111/J.1749-6632.2003.Tb07161.X |
0.563 |
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2003 |
Gerbasi V, Lutsenko S, Lewis EJ. A mutation in the ATP7B copper transporter causes reduced dopamine beta-hydroxylase and norepinephrine in mouse adrenal. Neurochemical Research. 28: 867-73. PMID 12718440 DOI: 10.1023/A:1023219308890 |
0.493 |
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2003 |
Ralle M, Lutsenko S, Blackburn NJ. X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines. The Journal of Biological Chemistry. 278: 23163-70. PMID 12686548 DOI: 10.1074/Jbc.M303474200 |
0.501 |
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2003 |
Huster D, Hoppert M, Lutsenko S, Zinke J, Lehmann C, Mössner J, Berr F, Caca K. Defective cellular localization of mutant ATP7B in Wilson's disease patients and hepatoma cell lines. Gastroenterology. 124: 335-45. PMID 12557139 DOI: 10.1053/Gast.2003.50066 |
0.442 |
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2003 |
Tsivkovskii R, Efremov RG, Lutsenko S. The role of the invariant His-1069 in folding and function of the Wilson's disease protein, the human copper-transporting ATPase ATP7B. The Journal of Biological Chemistry. 278: 13302-8. PMID 12551905 DOI: 10.1074/Jbc.M300034200 |
0.516 |
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2003 |
Lutsenko S, Petris MJ. Function and regulation of the mammalian copper-transporting ATPases: insights from biochemical and cell biological approaches. The Journal of Membrane Biology. 191: 1-12. PMID 12532272 DOI: 10.1007/S00232-002-1040-6 |
0.533 |
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2003 |
Blackburn NJ, Ralle M, Lutsenko S, Kaplan J, Eisses J, Stasser J. X-ray absorption studies of copper chaperones Journal of Inorganic Biochemistry. 96: 43. DOI: 10.1016/S0162-0134(03)80477-4 |
0.335 |
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2002 |
Lutsenko S, Efremov RG, Tsivkovskii R, Walker JM. Human copper-transporting ATPase ATP7B (the Wilson's disease protein): biochemical properties and regulation. Journal of Bioenergetics and Biomembranes. 34: 351-62. PMID 12539962 DOI: 10.1023/A:1021297919034 |
0.581 |
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2002 |
Vanderwerf SM, Lutsenko S. The Wilson's disease protein expressed in Sf9 cells is phosphorylated. Biochemical Society Transactions. 30: 739-41. PMID 12196182 DOI: 10.1042/Bst0300739 |
0.401 |
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2002 |
Walker JM, Tsivkovskii R, Lutsenko S. Metallochaperone Atox1 transfers copper to the NH2-terminal domain of the Wilson's disease protein and regulates its catalytic activity. The Journal of Biological Chemistry. 277: 27953-9. PMID 12029094 DOI: 10.1074/Jbc.M203845200 |
0.577 |
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2002 |
Tsivkovskii R, Eisses JF, Kaplan JH, Lutsenko S. Functional properties of the copper-transporting ATPase ATP7B (the Wilson's disease protein) expressed in insect cells. The Journal of Biological Chemistry. 277: 976-83. PMID 11677246 DOI: 10.1074/Jbc.M109368200 |
0.547 |
|
2001 |
Vanderwerf SM, Cooper MJ, Stetsenko IV, Lutsenko S. Copper specifically regulates intracellular phosphorylation of the Wilson's disease protein, a human copper-transporting ATPase. The Journal of Biological Chemistry. 276: 36289-94. PMID 11470780 DOI: 10.1074/Jbc.M102055200 |
0.553 |
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2001 |
Tsivkovskii R, MacArthur BC, Lutsenko S. The Lys1010–Lys1325 Fragment of the Wilson's Disease Protein Binds Nucleotides and Interacts with the N-terminal Domain of This Protein in a Copper-dependent Manner Journal of Biological Chemistry. 276: 2234-2242. PMID 11053407 DOI: 10.1074/Jbc.M003238200 |
0.463 |
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2000 |
Noll M, Lutsenko S. Expression of ZntA, a zinc-transporting P1-type ATPase, is specifically regulated by zinc and cadmium. Iubmb Life. 49: 297-302. PMID 10995032 DOI: 10.1080/15216540050033168 |
0.425 |
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1999 |
Buiakova OI, Xu J, Lutsenko S, Zeitlin S, Das K, Das S, Ross BM, Mekios C, Scheinberg IH, Gilliam TC. Null mutation of the murine ATP7B (Wilson disease) gene results in intracellular copper accumulation and late-onset hepatic nodular transformation. Human Molecular Genetics. 8: 1665-71. PMID 10441329 DOI: 10.1093/Hmg/8.9.1665 |
0.492 |
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1998 |
Noll M, Petrukhin K, Lutsenko S. Identification of a novel transcription regulator from Proteus mirabilis, PMTR, revealed a possible role of YJAI protein in balancing zinc in Escherichia coli. The Journal of Biological Chemistry. 273: 21393-401. PMID 9694902 DOI: 10.1074/Jbc.273.33.21393 |
0.387 |
|
1998 |
Lutsenko S, Cooper MJ. Localization of the Wilson’s disease protein product to mitochondria Proceedings of the National Academy of Sciences of the United States of America. 95: 6004-6009. PMID 9600907 DOI: 10.1073/Pnas.95.11.6004 |
0.456 |
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1998 |
Ralle M, Cooper MJ, Lutsenko S, Blackburn NJ. The menkes disease protein binds copper via novel 2-coordinate Cu(I)- cysteinates in the N-terminal domain [7] Journal of the American Chemical Society. 120: 13525-13526. DOI: 10.1021/Ja982990I |
0.507 |
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1997 |
Lutsenko S, Petrukhin K, Gilliam TC, Kaplan JH. Heterologous expression of the metal-binding domains of human copper-transporting ATPases (P1-ATPases). Annals of the New York Academy of Sciences. 834: 155-7. PMID 9405803 DOI: 10.1111/J.1749-6632.1997.Tb52246.X |
0.432 |
|
1997 |
Shah AB, Chernov I, Zhang HT, Ross BM, Das K, Lutsenko S, Parano E, Pavone L, Evgrafov O, Ivanova-Smolenskaya IA, Annerén G, Westermark K, Urrutia FH, Penchaszadeh GK, Sternlieb I, et al. Identification and analysis of mutations in the Wilson disease gene (ATP7B): population frequencies, genotype-phenotype correlation, and functional analyses. American Journal of Human Genetics. 61: 317-28. PMID 9311736 DOI: 10.1086/514864 |
0.386 |
|
1997 |
Lutsenko S, Petrukhin K, Cooper MJ, Gilliam CT, Kaplan JH. N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat. The Journal of Biological Chemistry. 272: 18939-44. PMID 9228074 DOI: 10.1074/Jbc.272.30.18939 |
0.525 |
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