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208 related items for PubMed ID: 11854285
1. Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase. Rodriguez JA, Valentine JS, Eggers DK, Roe JA, Tiwari A, Brown RH, Hayward LJ. J Biol Chem; 2002 May 03; 277(18):15932-7. PubMed ID: 11854285 [Abstract] [Full Text] [Related]
2. Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis. Hayward LJ, Rodriguez JA, Kim JW, Tiwari A, Goto JJ, Cabelli DE, Valentine JS, Brown RH. J Biol Chem; 2002 May 03; 277(18):15923-31. PubMed ID: 11854284 [Abstract] [Full Text] [Related]
11. Loss of in vitro metal ion binding specificity in mutant copper-zinc superoxide dismutases associated with familial amyotrophic lateral sclerosis. Goto JJ, Zhu H, Sanchez RJ, Nersissian A, Gralla EB, Valentine JS, Cabelli DE. J Biol Chem; 2000 Jan 14; 275(2):1007-14. PubMed ID: 10625639 [Abstract] [Full Text] [Related]
12. Denaturational stress induces formation of zinc-deficient monomers of Cu,Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis. Mulligan VK, Kerman A, Ho S, Chakrabartty A. J Mol Biol; 2008 Nov 07; 383(2):424-36. PubMed ID: 18761352 [Abstract] [Full Text] [Related]
13. Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation. Ray SS, Nowak RJ, Brown RH, Lansbury PT. Proc Natl Acad Sci U S A; 2005 Mar 08; 102(10):3639-44. PubMed ID: 15738401 [Abstract] [Full Text] [Related]
14. Reduced net charge and heterogeneity of pI isoforms in familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase. Roudeau S, Chevreux S, Carmona A, Ortega R. Electrophoresis; 2015 Oct 08; 36(19):2482-8. PubMed ID: 26084641 [Abstract] [Full Text] [Related]
15. Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis. Tiwari A, Hayward LJ. Neurodegener Dis; 2005 Oct 08; 2(3-4):115-27. PubMed ID: 16909016 [Abstract] [Full Text] [Related]
16. Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution. Banci L, Bertini I, D'Amelio N, Gaggelli E, Libralesso E, Matecko I, Turano P, Valentine JS. J Biol Chem; 2005 Oct 28; 280(43):35815-21. PubMed ID: 16105836 [Abstract] [Full Text] [Related]
17. Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation. Furukawa Y, O'Halloran TV. J Biol Chem; 2005 Apr 29; 280(17):17266-74. PubMed ID: 15691826 [Abstract] [Full Text] [Related]