Year |
Citation |
Score |
2003 |
DiDonato M, Craig L, Huff ME, Thayer MM, Cardoso RM, Kassmann CJ, Lo TP, Bruns CK, Powers ET, Kelly JW, Getzoff ED, Tainer JA. ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization. Journal of Molecular Biology. 332: 601-15. PMID 12963370 DOI: 10.1016/S0022-2836(03)00889-1 |
0.609 |
|
2003 |
DiDonato M, Craig L, Huff ME, Thayer MM, Cardoso RM, Kassmann CJ, Lo TP, Bruns CK, Powers ET, Kelly JW, Getzoff ED, Tainer JA. Erratum to “ALS Mutants of Human Superoxide Dismutase form Fibrous Aggregates via Framework Destabilization” [J. Mol. Biol. 332 (2003) 601–615] Journal of Molecular Biology. 334: 175. DOI: 10.1016/S0022-2836(03)01190-2 |
0.583 |
|
2002 |
Cardoso RM, Thayer MM, DiDonato M, Lo TP, Bruns CK, Getzoff ED, Tainer JA. Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase. Journal of Molecular Biology. 324: 247-56. PMID 12441104 DOI: 10.1016/S0022-2836(02)01090-2 |
0.546 |
|
1999 |
Mol CD, Parikh SS, Putnam CD, Lo TP, Tainer JA. DNA repair mechanisms for the recognition and removal of damaged DNA bases. Annual Review of Biophysics and Biomolecular Structure. 28: 101-28. PMID 10410797 DOI: 10.1146/Annurev.Biophys.28.1.101 |
0.43 |
|
1997 |
Zu JS, Deng HX, Lo TP, Mitsumoto H, Ahmed MS, Hung WY, Cai ZJ, Tainer JA, Siddique T. Exon 5 encoded domain is not required for the toxic function of mutant SOD1 but essential for the dismutase activity: identification and characterization of two new SOD1 mutations associated with familial amyotrophic lateral sclerosis. Neurogenetics. 1: 65-71. PMID 10735277 DOI: 10.1007/S100480050010 |
0.549 |
|
1997 |
Fisher CL, Cabelli DE, Hallewell RA, Beroza P, Lo TP, Getzoff ED, Tainer JA. Computational, pulse-radiolytic, and structural investigations of lysine-136 and its role in the electrostatic triad of human Cu,Zn superoxide dismutase. Proteins. 29: 103-12. PMID 9294870 DOI: 10.1002/(Sici)1097-0134(199709)29:1<103::Aid-Prot8>3.0.Co;2-G |
0.485 |
|
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