Year |
Citation |
Score |
2015 |
Chattopadhyay M, Nwadibia E, Strong CA, Gralla EB, Valentine JS, Whitelegge JP. The Disulfide Bond, but not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu-Zn Superoxide Dismutase (SOD1) Fibrillation. The Journal of Biological Chemistry. PMID 26511321 DOI: 10.1074/Jbc.M115.666503 |
0.411 |
|
2013 |
Chan PK, Chattopadhyay M, Sharma S, Souda P, Gralla EB, Borchelt DR, Whitelegge JP, Valentine JS. Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy. Proceedings of the National Academy of Sciences of the United States of America. 110: 10934-9. PMID 23781106 DOI: 10.1073/Pnas.1309613110 |
0.365 |
|
2012 |
Sheng Y, Chattopadhyay M, Whitelegge J, Valentine JS. SOD1 aggregation and ALS: role of metallation states and disulfide status. Current Topics in Medicinal Chemistry. 12: 2560-72. PMID 23339308 DOI: 10.2174/1568026611212220010 |
0.338 |
|
2011 |
Lelie HL, Liba A, Bourassa MW, Chattopadhyay M, Chan PK, Gralla EB, Miller LM, Borchelt DR, Valentine JS, Whitelegge JP. Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice. The Journal of Biological Chemistry. 286: 2795-806. PMID 21068388 DOI: 10.1074/Jbc.M110.186999 |
0.381 |
|
2009 |
Chattopadhyay M, Valentine JS. Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS. Antioxidants & Redox Signaling. 11: 1603-14. PMID 19271992 DOI: 10.1089/Ars.2009.2536 |
0.321 |
|
2008 |
Chattopadhyay M, Durazo A, Sohn SH, Strong CD, Gralla EB, Whitelegge JP, Valentine JS. Initiation and elongation in fibrillation of ALS-linked superoxide dismutase. Proceedings of the National Academy of Sciences of the United States of America. 105: 18663-8. PMID 19022905 DOI: 10.1073/Pnas.0807058105 |
0.448 |
|
2007 |
Dong J, Bloom JD, Goncharov V, Chattopadhyay M, Millhauser GL, Lynn DG, Scheibel T, Lindquist S. Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions. The Journal of Biological Chemistry. 282: 34204-12. PMID 17893150 DOI: 10.1074/Jbc.M704952200 |
0.527 |
|
2007 |
McCarthy P, Chattopadhyay M, Millhauser GL, Tsarevsky NV, Bombalski L, Matyjaszewski K, Shimmin D, Avdalovic N, Pohl C. Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides. Analytical Biochemistry. 366: 1-8. PMID 17481564 DOI: 10.1016/J.Ab.2007.03.008 |
0.505 |
|
2006 |
Walter ED, Chattopadhyay M, Millhauser GL. The affinity of copper binding to the prion protein octarepeat domain: evidence for negative cooperativity. Biochemistry. 45: 13083-92. PMID 17059225 DOI: 10.1021/Bi060948R |
0.604 |
|
2006 |
Fielding AJ, Fox S, Millhauser GL, Chattopadhyay M, Kroneck PM, Fritz G, Eaton GR, Eaton SS. Electron spin relaxation of copper(II) complexes in glassy solution between 10 and 120 K. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 179: 92-104. PMID 16343958 DOI: 10.1016/J.Jmr.2005.11.011 |
0.49 |
|
2005 |
Chattopadhyay M, Walter ED, Newell DJ, Jackson PJ, Aronoff-Spencer E, Peisach J, Gerfen GJ, Bennett B, Antholine WE, Millhauser GL. The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4. Journal of the American Chemical Society. 127: 12647-56. PMID 16144413 DOI: 10.1021/Ja053254Z |
0.575 |
|
Show low-probability matches. |