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Journal Abstract Search
243 related items for PubMed ID: 20404329
1. Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis. Furukawa Y, Kaneko K, Yamanaka K, Nukina N. J Biol Chem; 2010 Jul 16; 285(29):22221-31. PubMed ID: 20404329 [Abstract] [Full Text] [Related]
3. Wild-type Cu/Zn superoxide dismutase (SOD1) does not facilitate, but impedes the formation of protein aggregates of amyotrophic lateral sclerosis causing mutant SOD1. Witan H, Gorlovoy P, Kaya AM, Koziollek-Drechsler I, Neumann H, Behl C, Clement AM. Neurobiol Dis; 2009 Nov 16; 36(2):331-42. PubMed ID: 19660548 [Abstract] [Full Text] [Related]
6. Structural instability and Cu-dependent pro-oxidant activity acquired by the apo form of mutant SOD1 associated with amyotrophic lateral sclerosis. Kitamura F, Fujimaki N, Okita W, Hiramatsu H, Takeuchi H. Biochemistry; 2011 May 24; 50(20):4242-50. PubMed ID: 21506602 [Abstract] [Full Text] [Related]
7. Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy. Chan PK, Chattopadhyay M, Sharma S, Souda P, Gralla EB, Borchelt DR, Whitelegge JP, Valentine JS. Proc Natl Acad Sci U S A; 2013 Jul 02; 110(27):10934-9. PubMed ID: 23781106 [Abstract] [Full Text] [Related]
8. An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1. Prudencio M, Durazo A, Whitelegge JP, Borchelt DR. Hum Mol Genet; 2010 Dec 15; 19(24):4774-89. PubMed ID: 20871097 [Abstract] [Full Text] [Related]
9. Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis. Auclair JR, Boggio KJ, Petsko GA, Ringe D, Agar JN. Proc Natl Acad Sci U S A; 2010 Dec 14; 107(50):21394-9. PubMed ID: 21098299 [Abstract] [Full Text] [Related]
10. Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis. Rakhit R, Chakrabartty A. Biochim Biophys Acta; 2006 Dec 14; 1762(11-12):1025-37. PubMed ID: 16814528 [Abstract] [Full Text] [Related]
11. Superoxide dismutase 1 encoding mutations linked to ALS adopts a spectrum of misfolded states. Prudencio M, Borchelt DR. Mol Neurodegener; 2011 Nov 17; 6():77. PubMed ID: 22094223 [Abstract] [Full Text] [Related]
12. An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis. Ray SS, Nowak RJ, Strokovich K, Brown RH, Walz T, Lansbury PT. Biochemistry; 2004 May 04; 43(17):4899-905. PubMed ID: 15109247 [Abstract] [Full Text] [Related]
13. Copper chaperone for superoxide dismutase co-aggregates with superoxide dismutase 1 (SOD1) in neuronal Lewy body-like hyaline inclusions: an immunohistochemical study on familial amyotrophic lateral sclerosis with SOD1 gene mutation. Kato S, Sumi-Akamaru H, Fujimura H, Sakoda S, Kato M, Hirano A, Takikawa M, Ohama E. Acta Neuropathol; 2001 Sep 04; 102(3):233-8. PubMed ID: 11585247 [Abstract] [Full Text] [Related]
14. Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis. Furukawa Y, Kaneko K, Yamanaka K, O'Halloran TV, Nukina N. J Biol Chem; 2008 Aug 29; 283(35):24167-76. PubMed ID: 18552350 [Abstract] [Full Text] [Related]
15. Dimerization, oligomerization, and aggregation of human amyotrophic lateral sclerosis copper/zinc superoxide dismutase 1 protein mutant forms in live cells. Kim J, Lee H, Lee JH, Kwon DY, Genovesio A, Fenistein D, Ogier A, Brondani V, Grailhe R. J Biol Chem; 2014 May 23; 289(21):15094-103. PubMed ID: 24692554 [Abstract] [Full Text] [Related]
16. Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates. Ding F, Furukawa Y, Nukina N, Dokholyan NV. J Mol Biol; 2012 Aug 24; 421(4-5):548-60. PubMed ID: 22210350 [Abstract] [Full Text] [Related]