325 related articles for article (PubMed ID: 25666897)
1. 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; 1854(5):426-36. PubMed ID: 25666897
[TBL] [Abstract][Full Text] [Related]
2. 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; 7(2):333-46. PubMed ID: 25554447
[TBL] [Abstract][Full Text] [Related]
3. MIF inhibits the formation and toxicity of misfolded SOD1 amyloid aggregates: implications for familial ALS.
Shvil N; Banerjee V; Zoltsman G; Shani T; Kahn J; Abu-Hamad S; Papo N; Engel S; Bernhagen J; Israelson A
Cell Death Dis; 2018 Jan; 9(2):107. PubMed ID: 29371591
[TBL] [Abstract][Full Text] [Related]
4. Disruption of mitochondrial membrane integrity induced by amyloid aggregates arising from variants of SOD1.
Oladzad Abbasabadi A; Javanian A; Nikkhah M; Meratan AA; Ghiasi P; Nemat-Gorgani M
Int J Biol Macromol; 2013 Oct; 61():212-7. PubMed ID: 23872456
[TBL] [Abstract][Full Text] [Related]
5. 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; 4(3):e5004. PubMed ID: 19325915
[TBL] [Abstract][Full Text] [Related]
6. 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; 288(35):25219-25228. PubMed ID: 23861388
[TBL] [Abstract][Full Text] [Related]
7. 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; 75():290-7. PubMed ID: 25600987
[TBL] [Abstract][Full Text] [Related]
8. Calcium binding to gatekeeper residues flanking aggregation-prone segments underlies non-fibrillar amyloid traits in superoxide dismutase 1 (SOD1).
Estácio SG; Leal SS; Cristóvão JS; Faísca PF; Gomes CM
Biochim Biophys Acta; 2015 Feb; 1854(2):118-26. PubMed ID: 25463043
[TBL] [Abstract][Full Text] [Related]
9. Quercetin and Baicalein Act as Potent Antiamyloidogenic and Fibril Destabilizing Agents for SOD1 Fibrils.
Bhatia NK; Modi P; Sharma S; Deep S
ACS Chem Neurosci; 2020 Apr; 11(8):1129-1138. PubMed ID: 32208672
[TBL] [Abstract][Full Text] [Related]
10. 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; 290(51):30624-36. PubMed ID: 26511321
[TBL] [Abstract][Full Text] [Related]
11. Early steps in oxidation-induced SOD1 misfolding: implications for non-amyloid protein aggregation in familial ALS.
Mulligan VK; Kerman A; Laister RC; Sharda PR; Arslan PE; Chakrabartty A
J Mol Biol; 2012 Aug; 421(4-5):631-52. PubMed ID: 22542526
[TBL] [Abstract][Full Text] [Related]
12. Cu/Zn Superoxide Dismutase Forms Amyloid Fibrils under Near-Physiological Quiescent Conditions: The Roles of Disulfide Bonds and Effects of Denaturant.
Khan MAI; Respondek M; Kjellström S; Deep S; Linse S; Akke M
ACS Chem Neurosci; 2017 Sep; 8(9):2019-2026. PubMed ID: 28585802
[TBL] [Abstract][Full Text] [Related]
13. Nonnative SOD1 trimer is toxic to motor neurons in a model of amyotrophic lateral sclerosis.
Proctor EA; Fee L; Tao Y; Redler RL; Fay JM; Zhang Y; Lv Z; Mercer IP; Deshmukh M; Lyubchenko YL; Dokholyan NV
Proc Natl Acad Sci U S A; 2016 Jan; 113(3):614-9. PubMed ID: 26719414
[TBL] [Abstract][Full Text] [Related]
14. 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; 82(12):3356-72. PubMed ID: 25220364
[TBL] [Abstract][Full Text] [Related]
15. Intracellular seeded aggregation of mutant Cu,Zn-superoxide dismutase associated with amyotrophic lateral sclerosis.
Furukawa Y; Kaneko K; Watanabe S; Yamanaka K; Nukina N
FEBS Lett; 2013 Aug; 587(16):2500-5. PubMed ID: 23831581
[TBL] [Abstract][Full Text] [Related]
16. 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; 7(11):1595-1606. PubMed ID: 27540759
[TBL] [Abstract][Full Text] [Related]
17. Selective interception of gelsolin amyloidogenic stretch results in conformationally distinct aggregates with reduced toxicity.
Arya P; Srivastava A; Vasaikar SV; Mukherjee G; Mishra P; Kundu B
ACS Chem Neurosci; 2014 Oct; 5(10):982-92. PubMed ID: 25118567
[TBL] [Abstract][Full Text] [Related]
18. 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; 119(3):335-44. PubMed ID: 20111867
[TBL] [Abstract][Full Text] [Related]
19. Amyloidogenic regions in beta-strands II and III modulate the aggregation and toxicity of SOD1 in living cells.
McAlary L; Nan JR; Shyu C; Sher M; Plotkin SS; Cashman NR
Open Biol; 2024 Jun; 14(6):230418. PubMed ID: 38835240
[TBL] [Abstract][Full Text] [Related]
20. 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; 36(2):331-42. PubMed ID: 19660548
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
