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Journal Abstract Search
441 related items for PubMed ID: 23861388
1. Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non-fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)? Leal SS, Cardoso I, Valentine JS, Gomes CM. J Biol Chem; 2013 Aug 30; 288(35):25219-25228. PubMed ID: 23861388 [Abstract] [Full Text] [Related]
2. S100A6 amyloid fibril formation is calcium-modulated and enhances superoxide dismutase-1 (SOD1) aggregation. Botelho HM, Leal SS, Cardoso I, Yanamandra K, Morozova-Roche LA, Fritz G, Gomes CM. J Biol Chem; 2012 Dec 07; 287(50):42233-42. PubMed ID: 23076148 [Abstract] [Full Text] [Related]
4. Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase. Oztug Durer ZA, Cohlberg JA, Dinh P, Padua S, Ehrenclou K, Downes S, Tan JK, Nakano Y, Bowman CJ, Hoskins JL, Kwon C, Mason AZ, Rodriguez JA, Doucette PA, Shaw BF, Valentine JS. PLoS One; 2009 Feb 07; 4(3):e5004. PubMed ID: 19325915 [Abstract] [Full Text] [Related]
5. Curcumin binds to the pre-fibrillar aggregates of Cu/Zn superoxide dismutase (SOD1) and alters its amyloidogenic pathway resulting in reduced cytotoxicity. Bhatia NK, Srivastava A, Katyal N, Jain N, Khan MA, Kundu B, Deep S. Biochim Biophys Acta; 2015 May 07; 1854(5):426-36. PubMed ID: 25666897 [Abstract] [Full Text] [Related]
6. Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation. Leal SS, Cristóvão JS, Biesemeier A, Cardoso I, Gomes CM. Metallomics; 2015 Feb 07; 7(2):333-46. PubMed ID: 25554447 [Abstract] [Full Text] [Related]
7. Lipid molecules induce the cytotoxic aggregation of Cu/Zn superoxide dismutase with structurally disordered regions. Choi I, Yang YI, Song HD, Lee JS, Kang T, Sung JJ, Yi J. Biochim Biophys Acta; 2011 Jan 07; 1812(1):41-8. PubMed ID: 20837142 [Abstract] [Full Text] [Related]
8. Mitochondrial membrane disruption by aggregation products of ALS-causing superoxide dismutase-1 mutants. Salehi M, Nikkhah M, Ghasemi A, Arab SS. Int J Biol Macromol; 2015 Apr 07; 75():290-7. PubMed ID: 25600987 [Abstract] [Full Text] [Related]
9. Conformational Disorder of the Most Immature Cu, Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis. Furukawa Y, Anzai I, Akiyama S, Imai M, Cruz FJ, Saio T, Nagasawa K, Nomura T, Ishimori K. J Biol Chem; 2016 Feb 19; 291(8):4144-55. PubMed ID: 26694608 [Abstract] [Full Text] [Related]
10. A double point mutation of SOD1 targeting net charge promotes aggregation under destabilizing conditions: Correlation of charge distribution and ALS-provoking mutation. Mavadat E, Seyedalipour B, Hosseinkhani S. Biochim Biophys Acta Gen Subj; 2023 May 19; 1867(5):130325. PubMed ID: 36791828 [Abstract] [Full Text] [Related]
11. Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes. Pratt AJ, Shin DS, Merz GE, Rambo RP, Lancaster WA, Dyer KN, Borbat PP, Poole FL, Adams MW, Freed JH, Crane BR, Tainer JA, Getzoff ED. Proc Natl Acad Sci U S A; 2014 Oct 28; 111(43):E4568-76. PubMed ID: 25316790 [Abstract] [Full Text] [Related]
12. Toxic SOD1 trimers are off-pathway in the formation of amyloid-like fibrils in ALS. Hnath B, Dokholyan NV. Biophys J; 2022 Jun 07; 121(11):2084-2095. PubMed ID: 35505609 [Abstract] [Full Text] [Related]
13. Polyanion binding accelerates the formation of stable and low-toxic aggregates of ALS-linked SOD1 mutant A4V. Zhao D, Zhang S, Meng Y, Xiongwei D, Zhang D, Liang Y, Wang L, Liu C. Proteins; 2014 Dec 07; 82(12):3356-72. PubMed ID: 25220364 [Abstract] [Full Text] [Related]
14. Stochastic Formation of Fibrillar and Amorphous Superoxide Dismutase Oligomers Linked to Amyotrophic Lateral Sclerosis. Abdolvahabi A, Shi Y, Chuprin A, Rasouli S, Shaw BF. ACS Chem Neurosci; 2016 Jun 15; 7(6):799-810. PubMed ID: 26979728 [Abstract] [Full Text] [Related]
15. Glycerolipid Headgroups Control Rate and Mechanism of Superoxide Dismutase-1 Aggregation and Accelerate Fibrillization of Slowly Aggregating Amyotrophic Lateral Sclerosis Mutants. Rasouli S, Abdolvahabi A, Croom CM, Plewman DL, Shi Y, Shaw BF. ACS Chem Neurosci; 2018 Jul 18; 9(7):1743-1756. PubMed ID: 29649360 [Abstract] [Full Text] [Related]
17. The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation. Chattopadhyay M, Nwadibia E, Strong CD, Gralla EB, Valentine JS, Whitelegge JP. J Biol Chem; 2015 Dec 18; 290(51):30624-36. PubMed ID: 26511321 [Abstract] [Full Text] [Related]
18. Superoxide Dismutase 1 (SOD1)-Derived Peptide Inhibits Amyloid Aggregation of Familial Amyotrophic Lateral Sclerosis SOD1 Mutants. Banerjee V, Shani T, Katzman B, Vyazmensky M, Papo N, Israelson A, Engel S. ACS Chem Neurosci; 2016 Nov 16; 7(11):1595-1606. PubMed ID: 27540759 [Abstract] [Full Text] [Related]
19. Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form. Kerman A, Liu HN, Croul S, Bilbao J, Rogaeva E, Zinman L, Robertson J, Chakrabartty A. Acta Neuropathol; 2010 Mar 16; 119(3):335-44. PubMed ID: 20111867 [Abstract] [Full Text] [Related]
20. Large SOD1 aggregates, unlike trimeric SOD1, do not impact cell viability in a model of amyotrophic lateral sclerosis. Zhu C, Beck MV, Griffith JD, Deshmukh M, Dokholyan NV. Proc Natl Acad Sci U S A; 2018 May 01; 115(18):4661-4665. PubMed ID: 29666246 [Abstract] [Full Text] [Related] Page: [Next] [New Search]